6yb3
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Crystal structure of a native BcsRQ complex purified and crystallized in the absence of nucleotide== |
| - | <StructureSection load='6yb3' size='340' side='right'caption='[[6yb3]]' scene=''> | + | <StructureSection load='6yb3' size='340' side='right'caption='[[6yb3]], [[Resolution|resolution]] 1.59Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yb3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YB3 FirstGlance]. <br> |
| - | </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=6yb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yb3 OCA], [https://pdbe.org/6yb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yb3 RCSB], [https://www.ebi.ac.uk/pdbsum/6yb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yb3 ProSAT]</span></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]] 1.59Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6yb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yb3 OCA], [https://pdbe.org/6yb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yb3 RCSB], [https://www.ebi.ac.uk/pdbsum/6yb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yb3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BCSQ_ECOLI BCSQ_ECOLI] Essential for cellulose biosynthesis, shown for strain 1094, a commensal, natural cellulose producer (PubMed:19400787). Also shown in strain W3110 which has a restored reading frame (TAG stop codon to TTG for amino acid 6, called strain AR3110), this protein (PubMed:24097954). May play a role in subcellular localization of an active cellulose biosynthesis apparatus at the bacterial cell pole (PubMed:19400787). The combination of cellulose and the curli fiber network confer cohesion, elasticity and tissue-like properties to colonies (PubMed:24097954).<ref>PMID:19400787</ref> <ref>PMID:24097954</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many free-living and pathogenic enterobacteria secrete biofilm-promoting cellulose using a multicomponent, envelope-embedded Bcs secretion system under the control of intracellular second messenger c-di-GMP. The molecular understanding of system assembly and cellulose secretion has been largely limited to the crystallographic studies of a distantly homologous BcsAB synthase tandem and a low-resolution reconstruction of an assembled macrocomplex that encompasses most of the inner membrane and cytosolic subunits and features an atypical layered architecture. Here, we present cryo-EM structures of the assembled Bcs macrocomplex, as well as multiple crystallographic snapshots of regulatory Bcs subcomplexes. The structural and functional data uncover the mechanism of asymmetric secretion system assembly and periplasmic crown polymerization and reveal unexpected subunit stoichiometry, multisite c-di-GMP recognition, and ATP-dependent regulation. | ||
| + | |||
| + | Architecture and regulation of an enterobacterial cellulose secretion system.,Abidi W, Zouhir S, Caleechurn M, Roche S, Krasteva PV Sci Adv. 2021 Jan 27;7(5). pii: 7/5/eabd8049. doi: 10.1126/sciadv.abd8049. Print , 2021 Jan. PMID:33563593<ref>PMID:33563593</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6yb3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Abidi W]] |
| + | [[Category: Caleechurn M]] | ||
| + | [[Category: Krasteva PV]] | ||
| + | [[Category: Roche S]] | ||
| + | [[Category: Zouhir S]] | ||
Current revision
Crystal structure of a native BcsRQ complex purified and crystallized in the absence of nucleotide
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