5olt
From Proteopedia
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<StructureSection load='5olt' size='340' side='right' caption='[[5olt]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='5olt' size='340' side='right' caption='[[5olt]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5olt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OLT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5olt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OLT FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bcsG, STM3624 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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=5olt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5olt OCA], [http://pdbe.org/5olt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5olt RCSB], [http://www.ebi.ac.uk/pdbsum/5olt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5olt 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=5olt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5olt OCA], [http://pdbe.org/5olt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5olt RCSB], [http://www.ebi.ac.uk/pdbsum/5olt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5olt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BCSG_SALTY BCSG_SALTY]] Required for cellulose biosynthesis.<ref>PMID:11929533</ref> | [[http://www.uniprot.org/uniprot/BCSG_SALTY BCSG_SALTY]] Required for cellulose biosynthesis.<ref>PMID:11929533</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many bacteria secrete cellulose, which forms the structural basis for bacterial multicellular aggregates, termed biofilms. The cellulose synthase complex of Salmonella typhimurium consists of the catalytic subunits BcsA and BcsB and several auxiliary subunits that are encoded by two divergently transcribed operons, bcsRQABZC and bcsEFG. Expression of the bcsEFG operon is required for full-scale cellulose production, but the functions of its products are not fully understood. This work aimed to characterize the BcsG subunit of the cellulose synthase, which consists of an N-terminal transmembrane fragment and a C-terminal domain in the periplasm. Deletion of the bcsG gene substantially decreased the total amount of BcsA and cellulose production. BcsA levels were partially restored by the expression of the transmembrane segment, whereas restoration of cellulose production required the presence of the C-terminal periplasmic domain and its characteristic metal-binding residues. The high-resolution crystal structure of the periplasmic domain characterized BcsG as a member of the alkaline phosphatase/sulfatase superfamily of metalloenzymes, containing a conserved Zn(2+)-binding site. Sequence and structural comparisons showed that BcsG belongs to a specific family within alkaline phosphatase-like enzymes, which includes bacterial Zn(2+)-dependent lipopolysaccharide phosphoethanolamine transferases such as MCR-1 (colistin resistance protein), EptA, and EptC and the Mn(2+)-dependent lipoteichoic acid synthase (phosphoglycerol transferase) LtaS. These enzymes use the phospholipids phosphatidylethanolamine and phosphatidylglycerol, respectively, as substrates. These data are consistent with the recently discovered phosphoethanolamine modification of cellulose by BcsG and show that its membrane-bound and periplasmic parts play distinct roles in the assembly of the functional cellulose synthase and cellulose production. | ||
| + | |||
| + | Structural and Functional Characterization of the BcsG Subunit of the Cellulose Synthase in Salmonella typhimurium.,Sun L, Vella P, Schnell R, Polyakova A, Bourenkov G, Li F, Cimdins A, Schneider TR, Lindqvist Y, Galperin MY, Schneider G, Romling U J Mol Biol. 2018 Sep 14;430(18 Pt B):3170-3189. doi: 10.1016/j.jmb.2018.07.008., Epub 2018 Jul 12. PMID:30017920<ref>PMID:30017920</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5olt" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Salty]] | ||
[[Category: Bourenkov, G]] | [[Category: Bourenkov, G]] | ||
[[Category: Lindqvist, Y]] | [[Category: Lindqvist, Y]] | ||
Revision as of 07:32, 21 February 2019
Crystal structure of the extramembrane domain of the cellulose biosynthetic protein BcsG from Salmonella typhimurium
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