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6mgb

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Current revision (14:42, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6mgb' size='340' side='right'caption='[[6mgb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='6mgb' size='340' side='right'caption='[[6mgb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6mgb]] is a 1 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=6MGB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6mgb]] is a 1 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=6MGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MGB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TDIS_2046 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=999894 DSM 24515])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<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=6mgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgb OCA], [http://pdbe.org/6mgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgb RCSB], [http://www.ebi.ac.uk/pdbsum/6mgb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgb ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgb OCA], [https://pdbe.org/6mgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mgb RCSB], [https://www.ebi.ac.uk/pdbsum/6mgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgb ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A179D1D1_9BACT A0A179D1D1_9BACT]
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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--&gt;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--&gt;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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6mgb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dsm 24515]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Doyle, L]]
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[[Category: Thermosulfurimonas dismutans]]
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[[Category: Kimber, M S]]
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[[Category: Doyle L]]
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[[Category: Mallette, E]]
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[[Category: Kimber MS]]
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[[Category: Whitfield, C]]
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[[Category: Mallette E]]
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[[Category: Cytosine monophosphate]]
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[[Category: Whitfield C]]
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[[Category: Glycosyltransferase]]
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[[Category: Transferase]]
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Current revision

Thermosulfurimonas dismutans KpsC, beta Kdo 2,4 transferase

PDB ID 6mgb

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