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1nst

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(New page: 200px<br /> <applet load="1nst" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nst, resolution 2.3&Aring;" /> '''THE SULFOTRANSFERASE...)
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Revision as of 16:18, 12 November 2007

Image:1nst.gif

1nst, resolution 2.3Å

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THE SULFOTRANSFERASE DOMAIN OF HUMAN HAPARIN SULFATE N-DEACETYLASE/N-SULFOTRANSFERASE

Overview

Heparan sulfate N-deacetylase/N-sulfotransferase (HSNST) catalyzes the, first and obligatory step in the biosynthesis of heparan sulfates and, heparin. The crystal structure of the sulfotransferase domain (NST1) of, human HSNST-1 has been determined at 2.3-A resolution in a binary complex, with 3'-phosphoadenosine 5'-phosphate (PAP). NST1 is approximately, spherical with an open cleft, and consists of a single alpha/beta fold, with a central five-stranded parallel beta-sheet and a three-stranded, anti-parallel beta-sheet bearing an interstrand disulfide bond. The, structural regions alpha1, alpha6, beta1, beta7, 5'-phosphosulfate binding, loop (between beta1 and alpha1), and a random coil (between beta8 and, alpha13) constitute the PAP binding site of NST1. The alpha6 and random, coil (between beta2 and alpha2), which form an open cleft near the, 5'-phosphate of the PAP molecule, may provide interactions for substrate, binding. The conserved residue Lys-614 is in position to form a hydrogen, bond with the bridge oxygen of the 5'-phosphate.

About this Structure

1NST is a Single protein structure of sequence from Homo sapiens with A3P as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/ N-sulfotransferase 1., Kakuta Y, Sueyoshi T, Negishi M, Pedersen LC, J Biol Chem. 1999 Apr 16;274(16):10673-6. PMID:10196134

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