6bt4: Difference between revisions
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The | ==Crystal structure of the SLH domain of Sap from Bacillus anthracis in complex with a pyruvylated SCWP unit== | ||
<StructureSection load='6bt4' size='340' side='right' caption='[[6bt4]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6bt4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BT4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPM:2-(acetylamino)-4-O-{2-(acetylamino)-4,6-O-[(1S)-1-carboxyethylidene]-2-deoxy-beta-D-mannopyranosyl}-2-deoxy-beta-D-glucopyranose'>KPM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6bt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bt4 OCA], [http://pdbe.org/6bt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bt4 RCSB], [http://www.ebi.ac.uk/pdbsum/6bt4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bt4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SLAP1_BACAN SLAP1_BACAN]] The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial surface (S) layers are paracrystalline arrays of protein assembled on the bacterial cell wall that serve as protective barriers and scaffolds for housekeeping enzymes and virulence factors. The attachment of S-layer proteins to the cell walls of the Bacillus cereus sensu lato, which includes the pathogen Bacillus anthracis, occurs through noncovalent interactions between their S-layer homology domains and secondary cell wall polysaccharides. To promote these interactions, it is presumed that the terminal N-acetylmannosamine (ManNAc) residues of the secondary cell wall polysaccharides must be ketal-pyruvylated. For a few specific S-layer proteins, the O-acetylation of the penultimate N-acetylglucosamine (GlcNAc) is also required. Herein, we present the X-ray crystal structure of the SLH domain of the major surface array protein Sap from B. anthracis in complex with 4,6- O-ketal-pyruvyl-beta-ManNAc-(1,4)-beta-GlcNAc-(1,6)-alpha-GlcN. This structure reveals for the first time that the conserved terminal SCWP unit is the direct ligand for the SLH domain. Furthermore, we identify key binding interactions that account for the requirement of 4,6- O-ketal-pyruvyl-ManNAc while revealing the insignificance of the O-acetylation on the GlcNAc residue for recognition by Sap. | |||
Molecular Basis for the Attachment of S-Layer Proteins to the Cell Wall of Bacillus anthracis.,Sychantha D, Chapman RN, Bamford NC, Boons GJ, Howell PL, Clarke AJ Biochemistry. 2018 Mar 14. doi: 10.1021/acs.biochem.8b00060. PMID:29522326<ref>PMID:29522326</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6bt4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bamford, N C]] | |||
[[Category: Boons, G J]] | |||
[[Category: Chapman, R N]] | |||
[[Category: Clarke, A J]] | |||
[[Category: Howell, P L]] | |||
[[Category: Sychantha, D]] | |||
[[Category: Anthrax]] | |||
[[Category: Cell wall]] | |||
[[Category: S-layer]] | |||
[[Category: S-layer homology domain]] | |||
[[Category: Secondary cell wall polysaccharide]] | |||
[[Category: Structural protein]] | |||