7zcx
From Proteopedia
(Difference between revisions)
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==S-layer protein SlaA from Sulfolobus acidocaldarius at pH 4.0== | ==S-layer protein SlaA from Sulfolobus acidocaldarius at pH 4.0== | ||
| - | <StructureSection load='7zcx' size='340' side='right'caption='[[7zcx]], [[Resolution|resolution]] 3. | + | <StructureSection load='7zcx' size='340' side='right'caption='[[7zcx]], [[Resolution|resolution]] 3.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7zcx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZCX FirstGlance]. <br> | <table><tr><td colspan='2'>[[7zcx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZCX FirstGlance]. <br> | ||
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1Å</td></tr> |
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=YZT:6-deoxy-6-sulfo-beta-D-glucopyranose'>YZT</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=YZT:6-deoxy-6-sulfo-beta-D-glucopyranose'>YZT</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zcx OCA], [https://pdbe.org/7zcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zcx RCSB], [https://www.ebi.ac.uk/pdbsum/7zcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zcx ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zcx OCA], [https://pdbe.org/7zcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zcx RCSB], [https://www.ebi.ac.uk/pdbsum/7zcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zcx ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SLAA_SULAC SLAA_SULAC] S-layer large protein. May form the highly ordered outer sheath.[UniProtKB:Q980C7] | [https://www.uniprot.org/uniprot/SLAA_SULAC SLAA_SULAC] S-layer large protein. May form the highly ordered outer sheath.[UniProtKB:Q980C7] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
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| + | Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius.,Gambelli L, McLaren M, Conners R, Sanders K, Gaines MC, Clark L, Gold VAM, Kattnig D, Sikora M, Hanus C, Isupov MN, Daum B Elife. 2024 Jan 22;13:e84617. doi: 10.7554/eLife.84617. PMID:38251732<ref>PMID:38251732</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7zcx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
S-layer protein SlaA from Sulfolobus acidocaldarius at pH 4.0
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