Browse
Submit Data
Databases
API
Help

Dataset Information

13 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cryo-EM SPA dataset of Megadalton-range protein communities from a Chaetomium thermophilum native cell extract

ABSTRACT:

SUBMITTER: Panagiotis L. Kastritis

PROVIDER: EMPIAR-10892 | biostudies-other |

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Publications

Cryo-EM and artificial intelligence visualize endogenous protein community members.

Skalidis Ioannis I Kyrilis Fotis L FL Tüting Christian C Hamdi Farzad F Chojnowski Grzegorz G Kastritis Panagiotis L PL

Structure (London, England : 1993) 20220131 4

Cellular function is underlined by megadalton assemblies organizing in proximity, forming communities. Metabolons are protein communities involving metabolic pathways such as protein, fatty acid, and thioesters of coenzyme-A synthesis. Metabolons are highly heterogeneous due to their function, making their analysis particularly challenging. Here, we simultaneously characterize metabolon-embedded architectures of a 60S pre-ribosome, fatty acid synthase, and pyruvate/oxoglutarate dehydrogenase com ...[more]

PMID: 35093201

Publication: 1/2

Similar Datasets

Cryo-EM SPA dataset of 2-oxoglutarate dehydrogenase complex from a Chaetomium thermophilum native cell extract

Project description: Not available

| EMPIAR-11502 | biostudies-other

Cryo-EM SPA dataset of a native lysate fraction from human liver microsomes (fraction #1)

Project description: Not available

| EMPIAR-11249 | biostudies-other

Cryo-EM SPA dataset of a native lysate fraction from human liver microsomes (fraction #2)

Project description: Not available

| EMPIAR-11250 | biostudies-other

Cryo-EM study on a single, highly heterogeneous cellular fraction with megadalton complexes derived from Chaetomium thermophilum

Project description: Not available

| EMPIAR-11294 | biostudies-other

Cryo-EM structure of native human thyroglobulin.

Project description:The thyroglobulin (TG) protein is essential to thyroid hormone synthesis, plays a vital role in the regulation of metabolism, development and growth and serves as intraglandular iodine storage. Its architecture is conserved among vertebrates. Synthesis of triiodothyronine (T3) and thyroxine (T4) hormones depends on the conformation, iodination and post-translational modification of TG. Although structural information is available on recombinant and deglycosylated endogenous human thyroglobulin (hTG) from patients with goiters, the structure of native, fully glycosylated hTG remained unknown. Here, we present the cryo-electron microscopy structure of native and fully glycosylated hTG from healthy thyroid glands to 3.2 Å resolution. The structure provides detailed information on hormonogenic and glycosylation sites. We employ liquid chromatography-mass spectrometry (LC-MS) to validate these findings as well as other post-translational modifications and proteolytic cleavage sites. Our results offer insights into thyroid hormonogenesis of native hTG and provide a fundamental understanding of clinically relevant mutations.

| S-EPMC8748809 | biostudies-literature

Cryo-EM SPA dataset for Antibody SKV09 in complex with VEEV VLP (K3 movies/.tif files)

Project description: Not available

| EMPIAR-11338 | biostudies-other

Chaetomium thermophilum

Project description:Thermophilic fungus

| PRJNA47115 | ENA

Structural characterisation of the Chaetomium thermophilum Chl1 helicase.

Project description:Chl1 is a member of the XPD family of 5'-3' DNA helicases, which perform a variety of roles in genome maintenance and transmission. They possess a variety of unique structural features, including the presence of a highly variable, partially-ordered insertion in the helicase domain 1. Chl1 has been shown to be required for chromosome segregation in yeast due to its role in the formation of persistent chromosome cohesion during S-phase. Here we present structural and biochemical data to show that Chl1 has the same overall domain organisation as other members of the XPD family, but with some conformational alterations. We also present data suggesting the insert domain in Chl1 regulates its DNA binding.

| S-EPMC8109800 | biostudies-literature

Raw cryo- and negative stain micrographs of a native extract from C. thermophilum used to reconstruct oxo acid dehydrogenase complexes

Project description: Not available

| EMPIAR-10625 | biostudies-other

Cryo-EM structure of the native rhodopsin dimer in nanodiscs.

Project description:Imaging of rod photoreceptor outer-segment disc membranes by atomic force microscopy and cryo-electron tomography has revealed that the visual pigment rhodopsin, a prototypical class A G protein-coupled receptor (GPCR), can organize as rows of dimers. GPCR dimerization and oligomerization offer possibilities for allosteric regulation of GPCR activity, but the detailed structures and mechanism remain elusive. In this investigation, we made use of the high rhodopsin density in the native disc membranes and of a bifunctional cross-linker that preserves the native rhodopsin arrangement by covalently tethering rhodopsins via Lys residue side chains. We purified cross-linked rhodopsin dimers and reconstituted them into nanodiscs for cryo-EM analysis. We present cryo-EM structures of the cross-linked rhodopsin dimer as well as a rhodopsin dimer reconstituted into nanodiscs from purified monomers. We demonstrate the presence of a preferential 2-fold symmetrical dimerization interface mediated by transmembrane helix 1 and the cytoplasmic helix 8 of rhodopsin. We confirmed this dimer interface by double electron-electron resonance measurements of spin-labeled rhodopsin. We propose that this interface and the arrangement of two protomers is a prerequisite for the formation of the observed rows of dimers. We anticipate that the approach outlined here could be extended to other GPCRs or membrane receptors to better understand specific receptor dimerization mechanisms.

| S-EPMC6768649 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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