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| | <StructureSection load='6mgd' size='340' side='right'caption='[[6mgd]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6mgd' size='340' side='right'caption='[[6mgd]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mgd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_24515 Dsm 24515]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mgd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosulfurimonas_dismutans Thermosulfurimonas dismutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MGD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TDIS_1054 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=999894 DSM 24515])</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]] 2.5Å</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=6mgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgd OCA], [http://pdbe.org/6mgd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgd RCSB], [http://www.ebi.ac.uk/pdbsum/6mgd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgd ProSAT]</span></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=6mgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgd OCA], [https://pdbe.org/6mgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mgd RCSB], [https://www.ebi.ac.uk/pdbsum/6mgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A0A179D3Y0_9BACT A0A179D3Y0_9BACT] |
| - | Several important Gram-negative bacterial pathogens possess surface capsular layers composed of hypervariable long-chain polysaccharides linked via a conserved 3-deoxy-beta-D-manno-oct-2-ulosonic acid (beta-Kdo) oligosaccharide to a phosphatidylglycerol residue. The pathway for synthesis of the terminal glycolipid was elucidated by determining the structures of reaction intermediates. In Escherichia coli, KpsS transfers a single Kdo residue to phosphatidylglycerol; this primer is extended using a single enzyme (KpsC), possessing two cytidine 5'-monophosphate (CMP)-Kdo-dependent glycosyltransferase catalytic centers with different linkage specificities. The structure of the N-terminal beta-(2-->4) Kdo transferase from KpsC reveals two alpha/beta domains, supplemented by several helices. The N-terminal Rossmann-like domain, typically responsible for acceptor binding, is severely reduced in size compared with canonical GT-B folds in glycosyltransferases. The similar structure of the C-terminal beta-(2-->7) Kdo transferase indicates a past gene duplication event. Both Kdo transferases have a narrow active site tunnel, lined with key residues shared with GT99 beta-Kdo transferases. This enzyme provides the prototype for the GT107 family.
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| - | | + | |
| - | Biosynthesis of a conserved glycolipid anchor for Gram-negative bacterial capsules.,Doyle L, Ovchinnikova OG, Myler K, Mallette E, Huang BS, Lowary TL, Kimber MS, Whitfield C Nat Chem Biol. 2019 Jun;15(6):632-640. doi: 10.1038/s41589-019-0276-8. Epub 2019 , Apr 29. PMID:31036922<ref>PMID:31036922</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6mgd" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dsm 24515]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Doyle, L]] | + | [[Category: Thermosulfurimonas dismutans]] |
| - | [[Category: Kimber, M S]] | + | [[Category: Doyle L]] |
| - | [[Category: Mallette, E]] | + | [[Category: Kimber MS]] |
| - | [[Category: Whitfield, C]] | + | [[Category: Mallette E]] |
| - | [[Category: Cytosine monophosphate]]
| + | [[Category: Whitfield C]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
