4azv: Difference between revisions

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-'''Unreleased structure'''
-The entry 4azv is ON HOLD
+==Co-crystal structure of WbdD and kinase inhibitor GW435821x.==
+<StructureSection load='4azv' size='340' side='right'caption='[[4azv]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4azv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AZV FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ax8|4ax8]], [[4azs|4azs]], [[4azt|4azt]], [[4azw|4azw]]</div></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=4azv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azv OCA], [https://pdbe.org/4azv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4azv RCSB], [https://www.ebi.ac.uk/pdbsum/4azv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4azv ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Escherichia coli serotype O9a O-antigen polysaccharide (O-PS) is a model for glycan biosynthesis and export by the ATP-binding cassette transporter-dependent pathway. The polymannose O9a O-PS is synthesized as a polyprenol-linked glycan by mannosyltransferase enzymes located at the cytoplasmic membrane. The chain length of the O9a O-PS is tightly regulated by the WbdD enzyme. WbdD first phosphorylates the terminal non-reducing mannose of the O-PS and then methylates the phosphate, stopping polymerization. The 2.2 A resolution structure of WbdD reveals a bacterial methyltransferase domain joined to a eukaryotic kinase domain. The kinase domain is again fused to an extended C-terminal coiled-coil domain reminiscent of eukaryotic DMPK (Myotonic Dystrophy Protein Kinase) family kinases such as Rho-associated protein kinase (ROCK). WbdD phosphorylates 2-alpha-D-mannosyl-D-mannose (2alpha-MB), a short mimic of the O9a polymer. Mutagenesis identifies those residues important in catalysis and substrate recognition and the in vivo phenotypes of these mutants is used to dissect the termination reaction. We have determined the structures of co-complexes of WbdD with two known eukaryotic protein kinase inhibitors. Although these are potent inhibitors in vitro, they do not show any in vivo activity. The structures reveal new insight into O-PS chain-length regulation in this important model system.
-Authors: Hagelueken, G., Huang, H., Naismith, J.H.
+Structure of WbdD; a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in Escherichia coli O9a.,Hagelueken G, Huang H, Clarke BR, Lebl T, Whitfield C, Naismith JH Mol Microbiol. 2012 Sep 13. doi: 10.1111/mmi.12014. PMID:22970759<ref>PMID:22970759</ref>
-Description: Co-crystal structure of WbdD and kinase inhibitor GW435821x.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4azv" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Hagelueken, G]]
+[[Category: Huang, H]]
+[[Category: Naismith, J H]]
+[[Category: Methyltransferase]]
+[[Category: Transferase]]