2ra1
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ra1' size='340' side='right'caption='[[2ra1]], [[Resolution|resolution]] 2.41Å' scene=''> | <StructureSection load='2ra1' size='340' side='right'caption='[[2ra1]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ra1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2ra1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RA1 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.406Å</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=2ra1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ra1 OCA], [https://pdbe.org/2ra1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ra1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ra1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ra1 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=2ra1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ra1 OCA], [https://pdbe.org/2ra1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ra1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ra1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ra1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O68840_GEOSE O68840_GEOSE] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ra1 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ra1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Surface layers (S-layers) comprise the outermost cell envelope component of most archaea and many bacteria. Here we present the structure of the bacterial S-layer protein SbsC from Geobacillus stearothermophilus, showing a very elongated and flexible molecule, with strong and specific binding to the secondary cell wall polymer (SCWP). The crystal structure of rSbsC((31-844)) revealed a novel fold, consisting of six separate domains, which are connected by short flexible linkers. The N-terminal domain exhibits positively charged residues regularly spaced along the putative ligand binding site matching the distance of the negative charges on the extended SCWP. Upon SCWP binding, a considerable stabilization of the N-terminal domain occurs. These findings provide insight into the processes of S-layer attachment to the underlying cell wall and self-assembly, and also accommodate the observed mechanical strength, the polarity of the S-layer, and the pronounced requirement for surface flexibility inherent to cell growth and division. | ||
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| - | The structure and binding behavior of the bacterial cell surface layer protein SbsC.,Pavkov T, Egelseer EM, Tesarz M, Svergun DI, Sleytr UB, Keller W Structure. 2008 Aug 6;16(8):1226-37. PMID:18682224<ref>PMID:18682224</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2ra1" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Geobacillus stearothermophilus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Egelseer | + | [[Category: Egelseer EM]] |
| - | [[Category: Keller | + | [[Category: Keller W]] |
| - | [[Category: Pavkov | + | [[Category: Pavkov T]] |
| - | [[Category: Sleytr | + | [[Category: Sleytr UB]] |
| - | [[Category: Tesarz | + | [[Category: Tesarz M]] |
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Current revision
Crystal structure of the N-terminal part of the bacterial S-layer protein SbsC
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