2am5: Difference between revisions

Revision as of 15:26, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2am5.png

Template:STRUCTURE 2am5

Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDPCrystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP

Template:ABSTRACT PUBMED 16769084

About this StructureAbout this Structure

2AM5 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues., Gordon RD, Sivarajah P, Satkunarajah M, Ma D, Tarling CA, Vizitiu D, Withers SG, Rini JM, J Mol Biol. 2006 Jun 30;360(1):67-79. Epub 2006 May 12. PMID:16769084

Page seeded by OCA on Tue Jul 29 15:26:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP'''
+===Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP===
-==Overview==
+<!--
-The Golgi-resident glycosyltransferase, UDP-N-acetyl-d-glucosamine:alpha-3-d-mannoside beta-1,2-N-acetylglucosaminyltransferase I (GnT I), initiates the conversion of high-mannose oligosaccharides to complex and hybrid structures in the biosynthesis of N-linked glycans. Reported here are the X-ray crystal structures of GnT I in complex with UDP-CH2-GlcNAc (a non-hydrolyzable C-glycosidic phosphonate), UDP-2-deoxy-2-fluoro-glucose, UDP-glucose and UDP. Collectively, these structures provide evidence for the importance of the GlcNAc moiety and its N-acetyl group in donor substrate binding, as well as insight into the role played by the flexible 318-330 loop in substrate binding and product release. In addition, the UDP-CH2-GlcNAc complex reveals a well-defined glycerol molecule poised for nucleophilic attack on the C1 atom of the donor substrate analogue. The position and orientation of this glycerol molecule have allowed us to model the binding of the Manalpha1,3Manbeta1 moiety of the acceptor substrate and, based on the model, to suggest a rationalization for the main determinants of GnT I acceptor specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_16769084}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16769084 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16769084}}
 ==About this Structure==
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 [[Category: Udp]]
 [[Category: Udp-glcnac]]
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