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6cwn

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Current revision (14:31, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6cwn' size='340' side='right'caption='[[6cwn]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
<StructureSection load='6cwn' size='340' side='right'caption='[[6cwn]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6cwn]] is a 1 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=6CWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CWN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6cwn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_alvei Paenibacillus alvei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CWN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6LA:methyl+2-(acetylamino)-4,6-O-[(1S)-1-carboxyethylidene]-2-deoxy-beta-D-mannopyranoside'>6LA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cwc|6cwc]], [[6cwf|6cwf]], [[6cwh|6cwh]], [[6cwi|6cwi]], [[6cwl|6cwl]], [[6cwm|6cwm]], [[6cwr|6cwr]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6LA:methyl+2-(acetylamino)-4,6-O-[(1S)-1-carboxyethylidene]-2-deoxy-beta-D-mannopyranoside'>6LA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwn OCA], [https://pdbe.org/6cwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cwn RCSB], [https://www.ebi.ac.uk/pdbsum/6cwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwn ProSAT]</span></td></tr>
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<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=6cwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwn OCA], [http://pdbe.org/6cwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cwn RCSB], [http://www.ebi.ac.uk/pdbsum/6cwn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwn ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/C1JZ07_PAEAL C1JZ07_PAEAL]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6cwn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 6344]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Blackler, R J]]
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[[Category: Paenibacillus alvei]]
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[[Category: Evans, S V]]
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[[Category: Blackler RJ]]
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[[Category: S-layer]]
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[[Category: Evans SV]]
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[[Category: Scwp]]
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[[Category: Secondary cell wall polymer]]
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[[Category: Slh]]
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[[Category: Sugar binding protein]]
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[[Category: Surface layer homology domain]]
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Current revision

Crystal structure of SpaA-SLH/G109A in complex with 4,6-Pyr-beta-D-ManNAcOMe

PDB ID 6cwn

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