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New page: left|200px<br /> <applet load="1nst" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nst, resolution 2.3Å" /> '''THE SULFOTRANSFERASE...
 
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[[Image:1nst.gif|left|200px]]<br />
[[Image:1nst.gif|left|200px]]<br /><applet load="1nst" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1nst" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1nst, resolution 2.3&Aring;" />
caption="1nst, resolution 2.3&Aring;" />
'''THE SULFOTRANSFERASE DOMAIN OF HUMAN HAPARIN SULFATE N-DEACETYLASE/N-SULFOTRANSFERASE'''<br />
'''THE SULFOTRANSFERASE DOMAIN OF HUMAN HAPARIN SULFATE N-DEACETYLASE/N-SULFOTRANSFERASE'''<br />


==Overview==
==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.
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==
==About this Structure==
1NST is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with A3P as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NST OCA].  
1NST is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=A3P:'>A3P</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NST OCA].  


==Reference==
==Reference==
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[[Category: Kakuta, Y.]]
[[Category: Kakuta, Y.]]
[[Category: Negishi, M.]]
[[Category: Negishi, M.]]
[[Category: Pedersen, L.C.]]
[[Category: Pedersen, L C.]]
[[Category: A3P]]
[[Category: A3P]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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[[Category: sulfotransferase]]
[[Category: sulfotransferase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:25:01 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:36 2008''

Revision as of 12:09, 21 February 2008

File: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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