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3duv
From Proteopedia
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| - | [[Image:3duv.png|left|200px]] | ||
| - | + | ==Crystal structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate in the-configuration== | |
| + | <StructureSection load='3duv' size='340' side='right'caption='[[3duv]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3duv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DUV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kdsB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38] </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=3duv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3duv OCA], [https://pdbe.org/3duv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3duv RCSB], [https://www.ebi.ac.uk/pdbsum/3duv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3duv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/KDSB_HAEIN KDSB_HAEIN]] Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/du/3duv_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3duv ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzyme 3-deoxy-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase; CKS) catalyzes the activation of 3-deoxy-D-manno-octulosonate (or 2-keto-3-deoxy-manno-octonic acid; KDO) by forming CMP-KDO. CKS is unique to Gram-negative bacteria and is an attractive target for the development of antibacterial agents. The crystal structure of CKS from Haemophilus influenzae in complex with the substrate KDO has been determined at 2.30 A resolution by combining single-wavelength anomalous diffraction and molecular-replacement methods. The two monomers in the asymmetric unit differ in the conformation of their C-terminal alpha-helix (Ala230-Asn254). The KDO bound to the active site exists as the beta-pyranose form in the (5)C(2) chair conformation. The structure of CKS from H. influenzae in complex with KDO will be useful in structure-based inhibitor design. | ||
| - | + | Structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate in the beta-configuration.,Yoon HJ, Ku MJ, Mikami B, Suh SW Acta Crystallogr D Biol Crystallogr. 2008 Dec;64(Pt 12):1292-4. Epub 2008, Nov 18. PMID:19018107<ref>PMID:19018107</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | <div class="pdbe-citations 3duv" style="background-color:#fffaf0;"></div> |
| - | [[ | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacterium influenzae lehmann and neumann 1896]] | ||
[[Category: 3-deoxy-manno-octulosonate cytidylyltransferase]] | [[Category: 3-deoxy-manno-octulosonate cytidylyltransferase]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Ku, M J | + | [[Category: Ku, M J]] |
| - | [[Category: Mikami, B | + | [[Category: Mikami, B]] |
| - | [[Category: Suh, S W | + | [[Category: Suh, S W]] |
| - | [[Category: Yoon, H J | + | [[Category: Yoon, H J]] |
[[Category: 3-deoxy-manno-octulosonate]] | [[Category: 3-deoxy-manno-octulosonate]] | ||
[[Category: Cmp-kdo synthetase]] | [[Category: Cmp-kdo synthetase]] | ||
| + | [[Category: Cytoplasm]] | ||
[[Category: Kdsb]] | [[Category: Kdsb]] | ||
[[Category: Lipopolysaccharide biosynthesis]] | [[Category: Lipopolysaccharide biosynthesis]] | ||
[[Category: Nucleotidyltransferase]] | [[Category: Nucleotidyltransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Current revision
Crystal structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate in the-configuration
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Categories: Bacterium influenzae lehmann and neumann 1896 | 3-deoxy-manno-octulosonate cytidylyltransferase | Large Structures | Ku, M J | Mikami, B | Suh, S W | Yoon, H J | 3-deoxy-manno-octulosonate | Cmp-kdo synthetase | Cytoplasm | Kdsb | Lipopolysaccharide biosynthesis | Nucleotidyltransferase | Transferase
