6cwl
From Proteopedia
(Difference between revisions)
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<StructureSection load='6cwl' size='340' side='right' caption='[[6cwl]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='6cwl' size='340' side='right' caption='[[6cwl]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6cwl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CWL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cwl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_6344 Atcc 6344]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CWL FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FHY:(2S,4aR,6R,7S,8R,8aS)-7-(acetylamino)-6-({2-(acetylamino)-3-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-4,6-O-[(1S)-1-carboxylic+acidethylidene]-2-deoxy-beta-D-mannopyranosyl}oxy)-8-{[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]oxy}-2-methylhexahydro-2H-pyrano[3,2-d][1,3]dioxine-2-carboxylic+acid'>FHY</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FHY:(2S,4aR,6R,7S,8R,8aS)-7-(acetylamino)-6-({2-(acetylamino)-3-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-4,6-O-[(1S)-1-carboxylic+acidethylidene]-2-deoxy-beta-D-mannopyranosyl}oxy)-8-{[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]oxy}-2-methylhexahydro-2H-pyrano[3,2-d][1,3]dioxine-2-carboxylic+acid'>FHY</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cwc|6cwc]], [[6cwf|6cwf]], [[6cwh|6cwh]], [[6cwi|6cwi]], [[6cwm|6cwm]], [[6cwn|6cwn]], [[6cwr|6cwr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cwc|6cwc]], [[6cwf|6cwf]], [[6cwh|6cwh]], [[6cwi|6cwi]], [[6cwm|6cwm]], [[6cwn|6cwn]], [[6cwr|6cwr]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44250 ATCC 6344])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwl OCA], [http://pdbe.org/6cwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cwl RCSB], [http://www.ebi.ac.uk/pdbsum/6cwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwl ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwl OCA], [http://pdbe.org/6cwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cwl RCSB], [http://www.ebi.ac.uk/pdbsum/6cwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Self-assembling protein surface (S-) layers are common cell envelope structures of prokaryotes and have critical roles from structural maintenance to virulence. S-layers of Gram-positive bacteria are often attached through the interaction of S-layer homology (SLH) domain trimers with peptidoglycan-linked secondary cell wall polymers (SCWPs). Here we present an in-depth characterization of this interaction, with co-crystal structures of the three consecutive SLH domains from the Paenibacillus alvei S-layer protein SpaA with defined SCWP ligands. The most highly conserved SLH domain residue SLH-Gly29 is shown to enable a peptide backbone flip essential for SCWP binding in both biophysical and cellular experiments. Furthermore, we find that a significant domain movement mediates binding by two different sites in the SLH domain trimer, which may allow anchoring readjustment to relieve S-layer strain caused by cell growth and division. | ||
| + | |||
| + | Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei.,Blackler RJ, Lopez-Guzman A, Hager FF, Janesch B, Martinz G, Gagnon SML, Haji-Ghassemi O, Kosma P, Messner P, Schaffer C, Evans SV Nat Commun. 2018 Aug 7;9(1):3120. doi: 10.1038/s41467-018-05471-3. PMID:30087354<ref>PMID:30087354</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6cwl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 6344]] | ||
[[Category: Blackler, R J]] | [[Category: Blackler, R J]] | ||
[[Category: Evans, S V]] | [[Category: Evans, S V]] | ||
Revision as of 06:34, 22 August 2018
Crystal structure of SpaA-SLH in complex with beta-D-GlcNAc-(1->3)-4,6-Pyr-beta-D-ManNAcOMe
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