Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Sulfolobus acidocaldarius s-layer SlaA cryoET dataset

ABSTRACT:

SUBMITTER: Bertram Daum

PROVIDER: EMPIAR-11888 | biostudies-other |

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Publications

Structure of the two-component S-layer of the archaeon <i>Sulfolobus acidocaldarius</i>.

Gambelli Lavinia L McLaren Mathew M Conners Rebecca R Sanders Kelly K Gaines Matthew C MC Clark Lewis L Gold Vicki A M VAM Kattnig Daniel D Sikora Mateusz M Hanus Cyril C Isupov Michail N MN Daum Bertram B

eLife 20240122

Surface layers (S-layers) are resilient two-dimensional protein lattices that encapsulate many bacteria and most archaea. In archaea, S-layers usually form the only structural component of the cell wall and thus act as the final frontier between the cell and its environment. Therefore, S-layers are crucial for supporting microbial life. Notwithstanding their importance, little is known about archaeal S-layers at the atomic level. Here, we combined single-particle cryo electron microscopy, cryo e ...[more]

PMID: 38251732

Similar Datasets

Sulfolobus acidocaldarius s-layer SlaA

Project description: Not available

| EMPIAR-11788 | biostudies-other

Structure of the two-component S-layer of the archaeon <i>Sulfolobus acidocaldarius</i>.

Project description:Surface layers (S-layers) are resilient two-dimensional protein lattices that encapsulate many bacteria and most archaea. In archaea, S-layers usually form the only structural component of the cell wall and thus act as the final frontier between the cell and its environment. Therefore, S-layers are crucial for supporting microbial life. Notwithstanding their importance, little is known about archaeal S-layers at the atomic level. Here, we combined single-particle cryo electron microscopy, cryo electron tomography, and Alphafold2 predictions to generate an atomic model of the two-component S-layer of Sulfolobus acidocaldarius. The outer component of this S-layer (SlaA) is a flexible, highly glycosylated, and stable protein. Together with the inner and membrane-bound component (SlaB), they assemble into a porous and interwoven lattice. We hypothesise that jackknife-like conformational changes in SlaA play important roles in S-layer assembly.

| S-EPMC10903991 | biostudies-literature

UDP-sulfoquinovose formation by Sulfolobus acidocaldarius.

Project description:The UDP-sulfoquinovose synthase Agl3 from Sulfolobus acidocaldarius converts UDP-D-glucose and sulfite to UDP-sulfoquinovose, the activated form of sulfoquinovose required for its incorporation into glycoconjugates. Based on the amino acid sequence, Agl3 belongs to the short-chain dehydrogenase/reductase enzyme superfamily, together with SQD1 from Arabidopsis thaliana, the only UDP-sulfoquinovose synthase with known crystal structure. By comparison of sequence and structure of Agl3 and SQD1, putative catalytic amino acids of Agl3 were selected for mutational analysis. The obtained data suggest for Agl3 a modified dehydratase reaction mechanism. We propose that in vitro biosynthesis of UDP-sulfoquinovose occurs through an NAD(+)-dependent oxidation/dehydration/enolization/sulfite addition process. In the absence of a sulfur donor, UDP-D-glucose is converted via UDP-4-keto-D-glucose to UDP-D-glucose-5,6-ene, the structure of which was determined by (1)H and (13)C-NMR spectroscopy. During the redox reaction the cofactor remains tightly bound to Agl3 and participates in the reaction in a concentration-dependent manner. For the first time, the rapid initial electron transfer between UDP-D-glucose and NAD(+) could be monitored in a UDP-sulfoquinovose synthase. Deuterium labeling confirmed that dehydration of UDP-D-glucose occurs only from the enol form of UDP-4-keto-glucose. The obtained functional data are compared with those from other UDP-sulfoquinovose synthases. A divergent evolution of Agl3 from S. acidocaldarius is suggested.

| S-EPMC4388408 | biostudies-literature

Sulfolobus acidocaldarius phosphoproteome

Project description:Shotgun phosphoproteome of Sulfolobus acidocaldarius using PAciFIC technique. Briefly, proteins were denatured, alkylated, trypsine digestion, SCX separation Fractionated peptides were analysed on Bruker HCTultra. Data processing and bioinformatics: data from mass spectrometry were then extracted to mgf format using Bruker Data Analysis V4.0 with a MRM script, these were then were searched against the Sulfolobus acidocaldarius database (containing 2223 proteins) downloaded from NCBI in March 2010 using Phenyx V 2.6 (Genebio, Geneva). The searches were performed using parameters as follows: carbamidomethylation of cysteine (fixed modification), oxidation of methionine (variation), and phosphorylation of serine, tyrosine, threonine (variation), trypsin with 2 missed cleavages. Furthermore, other parameters such as parent, MS/MS, tolerances were set at 2.0 and 0.8 Da, respectively, whilst minimum peptide length, z-score, p-value and AC score were set at 5, 5.5, 10-5, and 5.5 respectively.

2014-04-15 | PXD000289 | Pride

Sulfolobus acidocaldarius

Project description:Identification of the Sulfolobus acidocaldarius small RNome and L7Ae-RNA interactome

| PRJNA373915 | ENA

Sulfolobus acidocaldarius

Project description:Sulfolobus acidocaldarius Raw sequence reads

| PRJNA1121029 | ENA

Sulfolobus acidocaldarius

Project description:Sulfolobus acidocaldarius Genome sequencing and assembly

| PRJNA304349 | ENA

Sulfolobus acidocaldarius

Project description:Sulfolobus acidocaldarius: Transcriptome of RNase aCPSF2 Mutant

| PRJNA213193 | ENA

Sulfolobus acidocaldarius

Project description:Transcriptome of S. acidocaldarius MW001 strain grown as biofilm or planktonic cells and transcriptomic profile of an RNaseR-treated S. acidocaldarius MW001 small RNA sample

| PRJNA388657 | ENA

Sulfolobus acidocaldarius

Project description:Extreme thermoacidophilic sulfur-oxidizing archaeon

| PRJNA35727 | ENA