2c84

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[[Image:2c84.png|left|200px]]
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==CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP==
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<StructureSection load='2c84' size='340' side='right' caption='[[2c84]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c84]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pasteurella_multocida Pasteurella multocida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C84 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C84 FirstGlance]. <br>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c83|2c83]]</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=2c84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c84 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c84 RCSB], [http://www.ebi.ac.uk/pdbsum/2c84 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PM0188 is a newly identified sialyltransferase from P. multocida which transfers sialic acid from cytidine 5'-monophosphonuraminic acid (CMP-NeuAc) to an acceptor sugar. Although sialyltransferases are involved in important biological functions like cell-cell recognition, cell differentiation and receptor-ligand interactions, little is known about their catalytic mechanism. Here, we report the X-ray crystal structures of PM0188 in the presence of an acceptor sugar and a donor sugar analogue, revealing the precise mechanism of sialic acid transfer. Site-directed mutagenesis, kinetic assays, and structural analysis show that Asp141, His311, Glu338, Ser355 and Ser356 are important catalytic residues; Asp141 is especially crucial as it acts as a general base. These complex structures provide insights into the mechanism of sialyltransferases and the structure-based design of specific inhibitors.
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{{STRUCTURE_2c84| PDB=2c84 | SCENE= }}
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Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar.,Kim DU, Yoo JH, Lee YJ, Kim KS, Cho HS BMB Rep. 2008 Jan 31;41(1):48-54. PMID:18304450<ref>PMID:18304450</ref>
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===CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP===
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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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{{ABSTRACT_PUBMED_18304450}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2c84]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pasteurella_multocida Pasteurella multocida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C84 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:018304450</ref><ref group="xtra">PMID:014730352</ref><ref group="xtra">PMID:016511286</ref><references group="xtra"/>
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[[Category: Pasteurella multocida]]
[[Category: Pasteurella multocida]]
[[Category: Cho, H S.]]
[[Category: Cho, H S.]]

Revision as of 12:01, 29 October 2014

CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP

2c84, resolution 2.31Å

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