2ihk: Difference between revisions
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|PDB= 2ihk |SIZE=350|CAPTION= <scene name='initialview01'>2ihk</scene>, resolution 1.90Å | |PDB= 2ihk |SIZE=350|CAPTION= <scene name='initialview01'>2ihk</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CSF:CYTIDINE-5'-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC ACID'>CSF</scene> | |LIGAND= <scene name='pdbligand=CSF:CYTIDINE-5'-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC+ACID'>CSF</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= Pm0188 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 Pasteurella multocida]) | |GENE= Pm0188 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 Pasteurella multocida]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ihj|2IHJ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihk OCA], [http://www.ebi.ac.uk/pdbsum/2ihk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ihk RCSB]</span> | |||
}} | }} | ||
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[[Category: Fisher, A J.]] | [[Category: Fisher, A J.]] | ||
[[Category: Ni, L.]] | [[Category: Ni, L.]] | ||
[[Category: cmp-3f(equatorial)-neu5ac sialyltransferase two-rossmann domain]] | [[Category: cmp-3f(equatorial)-neu5ac sialyltransferase two-rossmann domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:44:28 2008'' | ||
Revision as of 03:44, 31 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Pm0188 (Pasteurella multocida) | ||||||
| Activity: | Beta-galactoside alpha-2,3-sialyltransferase, with EC number 2.4.99.4 | ||||||
| Related: | 2IHJ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F(equatorial)-Neu5Ac bound
OverviewOverview
Sialyltransferases 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.
About this StructureAbout this Structure
2IHK is a Single protein structure of sequence from Pasteurella multocida. Full crystallographic information is available from OCA.
ReferenceReference
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
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