|
|
Line 3: |
Line 3: |
| <StructureSection load='6cwr' size='340' side='right'caption='[[6cwr]], [[Resolution|resolution]] 1.24Å' scene=''> | | <StructureSection load='6cwr' size='340' side='right'caption='[[6cwr]], [[Resolution|resolution]] 1.24Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6cwr]] 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=6CWR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CWR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cwr]] 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=6CWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CWR FirstGlance]. <br> |
- | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.24Å</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]], [[6cwl|6cwl]], [[6cwm|6cwm]], [[6cwn|6cwn]]</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=6cwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwr OCA], [https://pdbe.org/6cwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cwr RCSB], [https://www.ebi.ac.uk/pdbsum/6cwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwr 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=6cwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cwr OCA], [http://pdbe.org/6cwr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cwr RCSB], [http://www.ebi.ac.uk/pdbsum/6cwr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cwr ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/C1JZ07_PAEAL C1JZ07_PAEAL] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
Line 22: |
Line 23: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Atcc 6344]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Blackler, R J]] | + | [[Category: Paenibacillus alvei]] |
- | [[Category: Evans, S V]] | + | [[Category: Blackler RJ]] |
- | [[Category: Gagnon, S M.L]] | + | [[Category: Evans SV]] |
- | [[Category: Haji-Ghassemi, O]] | + | [[Category: Gagnon SML]] |
- | [[Category: S-layer]] | + | [[Category: Haji-Ghassemi O]] |
- | [[Category: Scwp]]
| + | |
- | [[Category: Secondary cell wall polymer]]
| + | |
- | [[Category: Slh]]
| + | |
- | [[Category: Sugar binding protein]]
| + | |
- | [[Category: Surface layer homology domain]]
| + | |
| Structural highlights
Function
C1JZ07_PAEAL
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Blackler RJ, Lopez-Guzman A, Hager FF, Janesch B, Martinz G, Gagnon SML, Haji-Ghassemi O, Kosma P, Messner P, Schaffer C, Evans SV. Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei. Nat Commun. 2018 Aug 7;9(1):3120. doi: 10.1038/s41467-018-05471-3. PMID:30087354 doi:http://dx.doi.org/10.1038/s41467-018-05471-3
|