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6cwl

From Proteopedia

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'''Unreleased structure'''
 
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The entry 6cwl is ON HOLD
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==Crystal structure of SpaA-SLH in complex with beta-D-GlcNAc-(1->3)-4,6-Pyr-beta-D-ManNAcOMe==
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<StructureSection load='6cwl' size='340' side='right'caption='[[6cwl]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6cwl]] is a 2 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=6CWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CWL FirstGlance]. <br>
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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]] 2.15&#8491;</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=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>
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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=6cwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwl OCA], [https://pdbe.org/6cwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cwl RCSB], [https://www.ebi.ac.uk/pdbsum/6cwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/C1JZ07_PAEAL C1JZ07_PAEAL]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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Authors:
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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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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6cwl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Paenibacillus alvei]]
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[[Category: Blackler RJ]]
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[[Category: Evans SV]]

Current revision

Crystal structure of SpaA-SLH in complex with beta-D-GlcNAc-(1->3)-4,6-Pyr-beta-D-ManNAcOMe

PDB ID 6cwl

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