1vkj: Difference between revisions

Revision as of 22:22, 28 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:1vkj.png

Template:STRUCTURE 1vkj

Crystal structure of heparan sulfate 3-O-sulfotransferase isoform 1 in the presence of PAPCrystal structure of heparan sulfate 3-O-sulfotransferase isoform 1 in the presence of PAP

Template:ABSTRACT PUBMED 15060080

About this StructureAbout this Structure

1VKJ is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 1s6t. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure and mutational analysis of heparan sulfate 3-O-sulfotransferase isoform 1., Edavettal SC, Lee KA, Negishi M, Linhardt RJ, Liu J, Pedersen LC, J Biol Chem. 2004 Jun 11;279(24):25789-97. Epub 2004 Apr 1. PMID:15060080

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

OCA

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-'''Crystal structure of heparan sulfate 3-O-sulfotransferase isoform 1 in the presence of PAP'''
+===Crystal structure of heparan sulfate 3-O-sulfotransferase isoform 1 in the presence of PAP===
-==Overview==
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-Heparan sulfate interacts with antithrombin, a protease inhibitor, to regulate blood coagulation. Heparan sulfate 3-O-sulfotransferase isoform 1 performs the crucial last step modification in the biosynthesis of anticoagulant heparan sulfate. This enzyme transfers the sulfuryl group (SO(3)) from 3'-phosphoadenosine 5'-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin. In this study, we report the crystal structure of 3-O-sulfotransferase isoform 1 at 2.5-A resolution in a binary complex with 3'-phosphoadenosine 5'-phosphate. This structure reveals residues critical for 3'-phosphoadenosine 5'-phosphosulfate binding and suggests residues required for the binding of heparan sulfate. In addition, site-directed mutagenesis analyses suggest that residues Arg-67, Lys-68, Arg-72, Glu-90, His-92, Asp-95, Lys-123, and Arg-276 are essential for enzymatic activity. Among these essential amino acid residues, we find that residues Arg-67, Arg-72, His-92, and Asp-95 are conserved in heparan sulfate 3-O-sulfotransferases but not in heparan N-deacetylase/N-sulfotransferase, suggesting a role for these residues in conferring substrate specificity. Results from this study provide information essential for understanding the biosynthesis of anticoagulant heparan sulfate and the general mechanism of action of heparan sulfate sulfotransferases.
+The line below this paragraph, {{ABSTRACT_PUBMED_15060080}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15060080 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15060080}}
 ==About this Structure==
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 [[Category: Papss]]
 [[Category: Sulfotransferase]]
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