View source for 6cwf


==Crystal structure of SpaA-SLH in complex with 4,6-Pyr-beta-D-ManNAcOMe==
<StructureSection load='6cwf' size='340' side='right'caption='[[6cwf]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cwf]] 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=6CWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CWF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
<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></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=6cwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwf OCA], [https://pdbe.org/6cwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cwf RCSB], [https://www.ebi.ac.uk/pdbsum/6cwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C1JZ07_PAEAL C1JZ07_PAEAL] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6cwf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paenibacillus alvei]]
[[Category: Blackler RJ]]
[[Category: Evans SV]]