Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Stock-based detection of protein oligomeric states in jsPISA.

ABSTRACT: A new version of the popular software PISA for the analysis of macromolecular interfaces and identification of biological assemblies (complexes) from macromolecular crystal structures is presented. The new web server jsPISA has a substantially improved user interface, based on modern JavaScript technologies, and also new elements of analysis: assembly stock and interaction radar. The new elements help interpretation of PISA results in difficult and ambiguous cases, for example, when the oligomeric state depends on protein concentration, or when the biologically relevant interaction is weak and cannot be easily discriminated from superficial crystal contacts. jsPISA is maintained by CCP4 at http://www.ccp4.ac.uk/pisa. There are no login requirements for using the server.

SUBMITTER: Krissinel E

PROVIDER: S-EPMC4489313 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Stock-based detection of protein oligomeric states in jsPISA.

Krissinel Eugene E

Nucleic acids research 20150423 W1

A new version of the popular software PISA for the analysis of macromolecular interfaces and identification of biological assemblies (complexes) from macromolecular crystal structures is presented. The new web server jsPISA has a substantially improved user interface, based on modern JavaScript technologies, and also new elements of analysis: assembly stock and interaction radar. The new elements help interpretation of PISA results in difficult and ambiguous cases, for example, when the oligomer ...[more]

PMID: 25908787

Similar Datasets

Diverse oligomeric states of CEACAM IgV domains.

Project description:Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) comprise a large family of cell surface adhesion molecules that bind to themselves and other family members to carry out numerous cellular functions, including proliferation, signaling, differentiation, tumor suppression, and survival. They also play diverse and significant roles in immunity and infection. The formation of CEACAM oligomers is caused predominantly by interactions between their N-terminal IgV domains. Although X-ray crystal structures of CEACAM IgV domain homodimers have been described, how CEACAMs form heterodimers or remain monomers is poorly understood. To address this key aspect of CEACAM function, we determined the crystal structures of IgV domains that form a homodimeric CEACAM6 complex, monomeric CEACAM8, and a heterodimeric CEACAM6-CEACAM8 complex. To confirm and quantify these interactions in solution, we used analytical ultracentrifugation to measure the dimerization constants of CEACAM homodimers and isothermal titration calorimetry to determine the thermodynamic parameters and binding affinities of CEACAM heterodimers. We found the CEACAM6-CEACAM8 heterodimeric state to be substantially favored energetically relative to the CEACAM6 homodimer. Our data provide a molecular basis for the adoption of the diverse oligomeric states known to exist for CEACAMs and suggest ways in which CEACAM6 and CEACAM8 regulate the biological functions of one another, as well as of additional CEACAMs with which they interact, both in cis and in trans.

| S-EPMC4640789 | biostudies-literature

Oligomeric complexes formed by Redβ single strand annealing protein in its different DNA bound states.

Project description:Redβ is a single strand annealing protein from bacteriophage λ that binds loosely to ssDNA, not at all to pre-formed dsDNA, but tightly to a duplex intermediate of annealing. As viewed by electron microscopy, Redβ forms oligomeric rings on ssDNA substrate, and helical filaments on the annealed duplex intermediate. However, it is not clear if these are the functional forms of the protein in vivo. We have used size-exclusion chromatography coupled with multi-angle light scattering, analytical ultracentrifugation and native mass spectrometry (nMS) to characterize the size of the oligomers formed by Redβ in its different DNA-bound states. The nMS data, which resolve species with the highest resolution, reveal that Redβ forms an oligomer of 12 subunits in the absence of DNA, complexes ranging from 4 to 14 subunits on 38-mer ssDNA, and a much more distinct and stable complex of 11 subunits on 38-mer annealed duplex. We also measure the concentration of Redβ in cells active for recombination and find it to range from 7 to 27 μM. Collectively, these data provide new insights into the dynamic nature of the complex on ssDNA, and the more stable and defined complex on annealed duplex.

| S-EPMC8034648 | biostudies-literature

GCN-based stock relations analysis for stock market prediction.

Project description:Most stock price predictive models merely rely on the target stock's historical information to forecast future prices, where the linkage effects between stocks are neglected. However, a group of prior studies has shown that the leverage of correlations between stocks could significantly improve the predictions. This article proposes a unified time-series relational multi-factor model (TRMF), which composes a self-generating relations (SGR) algorithm that can extract relational features automatically. In addition, the TRMF model integrates stock relations with other multiple dimensional features for the price prediction compared to extant works. Experimental validations are performed on the NYSE and NASDAQ data, where the model is compared with the popular methods such as attention Long Short-Term Memory network (Attn-LSTM), Support Vector Regression (SVR), and multi-factor framework (MF). Results show that compared with these extant methods, our model has a higher expected cumulative return rate and a lower risk of return volatility.

| S-EPMC9455286 | biostudies-literature

Bacterial flagellar capping proteins adopt diverse oligomeric states.

Project description:Flagella are crucial for bacterial motility and pathogenesis. The flagellar capping protein (FliD) regulates filament assembly by chaperoning and sorting flagellin (FliC) proteins after they traverse the hollow filament and exit the growing flagellum tip. In the absence of FliD, flagella are not formed, resulting in impaired motility and infectivity. Here, we report the 2.2 Å resolution X-ray crystal structure of FliD from Pseudomonas aeruginosa, the first high-resolution structure of any FliD protein from any bacterium. Using this evidence in combination with a multitude of biophysical and functional analyses, we find that Pseudomonas FliD exhibits unexpected structural similarity to other flagellar proteins at the domain level, adopts a unique hexameric oligomeric state, and depends on flexible determinants for oligomerization. Considering that the flagellin filaments on which FliD oligomers are affixed vary in protofilament number between bacteria, our results suggest that FliD oligomer stoichiometries vary across bacteria to complement their filament assemblies.

| S-EPMC5072837 | biostudies-literature

Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPN<sup>+</sup> Proteases.

Project description:JAMM/MPN+ metalloproteases cleave (iso)peptide bonds C-terminal to ubiquitin (Ub) and ubiquitin-like protein (Ubl) domains and typically require association with protein partners for activity, which has limited a molecular understanding of enzyme function. To provide an insight, we solved the X-ray crystal structures of a catalytically active Pyrococcus furiosus JAMM/MPN+ metalloprotease (PfJAMM1) alone and in complex with a Ubl (PfSAMP2) to 1.7- to 1.9-Å resolution. PfJAMM1 was found to have a redox sensitive dimer interface. In the PfJAMM1-bound state of the SAMP2, a Ubl-to-Ub conformational change was detected. Surprisingly, distant homologs of PfJAMM1 were found to be closely related in 3D structure, including the interface for Ubl/Ub binding. From this work, we infer the molecular basis of how JAMM/MPN+ proteases recognize and cleave Ubl/Ub tags from diverse proteins and highlight an α2-helix structural element that is conserved and crucial for binding and removing the Ubl SAMP2 tag.

| S-EPMC5831132 | biostudies-literature

Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states.

Project description:The main principles of protein-protein recognition are elucidated by the studies of homooligomers which in turn mediate and regulate gene expression, activity of enzymes, ion channels, receptors, and cell-cell adhesion processes. Here we explore oligomeric states of homologous proteins in various organisms to better understand the functional roles and evolutionary mechanisms of homooligomerization. We observe a great diversity in mechanisms controlling oligomerization and focus in our study on insertions and deletions in homologous proteins and how they enable or disable complex formation. We show that insertions and deletions which differentiate monomers and dimers have a significant tendency to be located on the interaction interfaces and about a quarter of all proteins studied and forty percent of enzymes have regions which mediate or disrupt the formation of oligomers. We suggest that relatively small insertions or deletions may have a profound effect on complex stability and/or specificity. Indeed removal of complex enabling regions from protein structures in many cases resulted in the complete or partial loss of stability. Moreover, we find that insertions and deletions modulating oligomerization have a lower aggregation propensity and contain a larger fraction of polar, charged residues, glycine and proline compared to conventional interfaces and protein surface. Most likely, these regions may mediate specific interactions, prevent nonspecific dysfunctional aggregation and preclude undesired interactions between close paralogs therefore separating their functional pathways. Last, we show how the presence or absence of insertions and deletions on interfaces might be of practical value in annotating protein oligomeric states.

| S-EPMC2996646 | biostudies-literature

Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK).

Project description:The molecular chaperone DnaK binds to exposed hydrophobic segments in proteins, protecting them from aggregation. DnaK interacts with protein substrates via its substrate-binding domain, and the affinity of this interaction is allosterically regulated by its nucleotide-binding domain. In addition to regulating interdomain allostery, the nucleotide state has been found to influence homo-oligomerization of DnaK. However, the architecture of oligomeric DnaK and its potential functional relevance in the chaperone cycle remain undefined. Towards that goal, we examined the structures of DnaK by negative stain electron microscopy. We found that DnaK samples contain an ensemble of monomers, dimers, and other small, defined multimers. To better understand the function of these oligomers, we stabilized them by cross-linking and found that they retained ATPase activity and protected a model substrate from denaturation. However, these oligomers had a greatly reduced ability to refold substrate and did not respond to stimulation by DnaJ. Finally, we observed oligomeric DnaK in Escherichia coli cellular lysates by native gel electrophoresis and found that these structures became noticeably more prevalent in cells exposed to heat shock. Together, these studies suggest that DnaK oligomers are composed of ordered multimers that are functionally distinct from monomeric DnaK. Thus, oligomerization of DnaK might be an important step in chaperone cycling.

| S-EPMC3312962 | biostudies-literature

Drivers and rates of stock assessments in the United States.

Project description:Fisheries management is most effective when based on scientific estimates of sustainable fishing rates. While some simple approaches allow estimation of harvest limits, more data-intensive stock assessments are generally required to evaluate the stock's biomass and fishing rates relative to sustainable levels. Here we evaluate how stock characteristics relate to the rate of new assessments in the United States. Using a statistical model based on time-to-event analysis and 569 coastal marine fish and invertebrate stocks landed in commercial fisheries, we quantify the impact of region, habitat, life-history, and economic factors on the annual probability of being assessed. Although the majority of landings come from assessed stocks in all regions, less than half of the regionally-landed species currently have been assessed. As expected, our time-to-event model identified landed tonnage and ex-vessel price as the dominant factors determining increased rates of new assessments. However, we also found that after controlling for landings and price, there has been a consistent bias towards assessing larger-bodied species. A number of vulnerable groups such as rockfishes (Scorpaeniformes) and groundsharks (Carcharhiniformes) have a relatively high annual probability of being assessed after controlling for their relatively small tonnage and low price. Due to relatively low landed tonnage and price of species that are currently unassessed, our model suggests that the number of assessed stocks will increase more slowly in future decades.

| S-EPMC5947900 | biostudies-literature

Dissecting Oligomeric States with Photoactivated Localization Microscopy: A Numerical Model.

Project description:Although photoactivated localization microscopy offers the potential to interrogate protein interactions in the physiological environment of a cell, uncertainties in the detection efficiency of photoactivatable proteins lead to complications with data interpretation. Here, we present a numerical model that provides probabilities to detect neighboring molecules dependent on their oligomerization status, density, detection efficiency, and radius, and can be used to assess oligomeric states or detection efficiencies of two molecular species. © 2020 The Authors. Cytometry Part A published by Wiley Periodicals, Inc. on behalf of International Society for Advancement of Cytometry.

| S-EPMC7754424 | biostudies-literature

Aldolases Utilize Different Oligomeric States To Preserve Their Functional Dynamics.

Project description:Aldolases are essential enzymes in the glycolysis pathway and catalyze the reaction cleaving fructose/tagatose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. To determine how the aldolase motions relate to its catalytic process, we studied the dynamics of three different class II aldolase structures through simulations. We employed coarse-grained elastic network normal-mode analyses to investigate the dynamics of Escherichia coli fructose 1,6-bisphosphate aldolase, E. coli tagatose 1,6-bisphosphate aldolase, and Thermus aquaticus fructose 1,6-bisphosphate aldolase and compared their motions in different oligomeric states. The first one is a dimer, and the second and third are tetramers. Our analyses suggest that oligomerization not only stabilizes the aldolase structures, showing fewer fluctuations at the subunit interfaces, but also allows the enzyme to achieve the required dynamics for its functional loops. The essential mobility of these loops in the functional oligomeric states can facilitate the enzymatic mechanism, substrate recruitment in the open state, bringing the catalytic residues into their required configuration in the closed bound state, and moving back to the open state to release the catalytic products and repositioning the enzyme for its next catalytic cycle. These findings suggest that the aldolase global motions are conserved among aldolases having different oligomeric states to preserve its catalytic mechanism. The coarse-grained approaches taken permit an unprecedented view of the changes in the structural dynamics and how these relate to the critical structural stabilities essential for catalysis. The results are supported by experimental findings from many previous studies.

| S-EPMC6662587 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data