2c84
From Proteopedia
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- | [[Image:2c84.png|left|200px]] | ||
- | < | + | ==CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP== |
- | + | <StructureSection load='2c84' size='340' side='right'caption='[[2c84]], [[Resolution|resolution]] 2.31Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2c84]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2C84 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2c84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c84 OCA], [https://pdbe.org/2c84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c84 RCSB], [https://www.ebi.ac.uk/pdbsum/2c84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c84 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q15KI8_PASMD Q15KI8_PASMD] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2c84" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
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[[Category: Pasteurella multocida]] | [[Category: Pasteurella multocida]] | ||
- | [[Category: Cho | + | [[Category: Cho HS]] |
- | [[Category: Kim | + | [[Category: Kim DU]] |
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Current revision
CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP
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