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2c84

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[[Image:2c84.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP==
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|PDB= 2c84 |SIZE=350|CAPTION= <scene name='initialview01'>2c84</scene>, resolution 2.31&Aring;
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<StructureSection load='2c84' size='340' side='right'caption='[[2c84]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Binding+Site+For+Residue+C+A+1414'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<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>
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|ACTIVITY=
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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]] 2.31&#8491;</td></tr>
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|GENE=
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<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>
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|DOMAIN=
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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=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>
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|RELATEDENTRY=[[2c83|2C83]]
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</table>
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|RESOURCES=<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.ebi.ac.uk/pdbsum/2c84 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c84 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q15KI8_PASMD Q15KI8_PASMD]
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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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'''CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP'''
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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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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 2c84" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2C84 is a [[Single protein]] structure of 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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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18304450 18304450]
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[[Category: Pasteurella multocida]]
[[Category: Pasteurella multocida]]
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[[Category: Single protein]]
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[[Category: Cho HS]]
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[[Category: Cho, H S.]]
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[[Category: Kim DU]]
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[[Category: Kim, D U.]]
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[[Category: cmp]]
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[[Category: glycosyltransferase]]
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[[Category: hypothetical protein]]
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[[Category: pm0188]]
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[[Category: sialyltransferase]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:46 2008''
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Current revision

CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE PM0188 WITH CMP

PDB ID 2c84

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