2ihj: Difference between revisions
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==crystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F-Neu5Ac bound== | ==crystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F-Neu5Ac bound== | ||
<StructureSection load='2ihj' size='340' side='right' caption='[[2ihj]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2ihj' size='340' side='right' caption='[[2ihj]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pm0188 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 "Bacterium multocidum" Lehmann and Neumann 1899])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pm0188 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 "Bacterium multocidum" Lehmann and Neumann 1899])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactoside_alpha-2,3-sialyltransferase Beta-galactoside alpha-2,3-sialyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.4 2.4.99.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactoside_alpha-2,3-sialyltransferase Beta-galactoside alpha-2,3-sialyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.4 2.4.99.4] </span></td></tr> | ||
<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=2ihj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihj OCA], [http://pdbe.org/2ihj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ihj RCSB], [http://www.ebi.ac.uk/pdbsum/2ihj PDBsum]</span></td></tr> | <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=2ihj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihj OCA], [http://pdbe.org/2ihj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ihj RCSB], [http://www.ebi.ac.uk/pdbsum/2ihj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ihj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2ihj" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2ihj" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Sialyltransferase|Sialyltransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:24, 4 July 2018
crystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F-Neu5Ac boundcrystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F-Neu5Ac bound
Structural highlights
Publication Abstract from PubMedSialyltransferases are key enzymes involved in the biosynthesis of biologically and pathologically important sialic acid-containing molecules in nature. Binary X-ray crystal structures of a multifunctional Pasteurella multocida sialyltransferase (Delta24PmST1) with a donor analogue CMP-3F(a)Neu5Ac or CMP-3F(e)Neu5Ac were determined at 2.0 and 1.9 A resolutions, respectively. Ternary X-ray structures of the protein in complex with CMP or a donor analogue CMP-3F(a)Neu5Ac and an acceptor lactose have been determined at 2.0 and 2.27 A resolutions, respectively. This represents the first sialyltransferase structure and the first GT-B-type glycosyltransferase structure that is bound to both a donor analogue and an acceptor simultaneously. The four structures presented here reveal that binding of the nucleotide-activated donor sugar causes a buried tryptophan to flip out of the protein core to interact with the donor sugar and helps define the acceptor sugar binding site. Additionally, key amino acid residues involved in the catalysis have been identified. Structural and kinetic data support a direct displacement mechanism involving an oxocarbenium ion-like transition state assisted with Asp141 serving as a general base to activate the acceptor hydroxyl group. Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogues reveal substrate binding sites and catalytic mechanism.,Ni L, Chokhawala HA, Cao H, Henning R, Ng L, Huang S, Yu H, Chen X, Fisher AJ Biochemistry. 2007 May 29;46(21):6288-98. Epub 2007 May 8. PMID:17487984[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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