1NST

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

Summary for 1NST

• Entry DOI: 10.2210/pdb1nst/pdb
• Descriptor: HEPARAN SULFATE N-DEACETYLASE/N-SULFOTRANSFERASE, ADENOSINE-3'-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: sulfotransferase, pap, haparin sulfate, haparin sulfate biosynthesis, glycoprotein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 38344.45

Authors

Kakuta, Y.,Pedersen, L.C.,Negishi, M. (deposition date: 1998-09-07, release date: 1999-09-16, Last modification date: 2024-10-16)

Primary citation

Kakuta, Y.,Sueyoshi, T.,Negishi, M.,Pedersen, L.C.
Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/ N-sulfotransferase 1.
J.Biol.Chem., 274:10673-10676, 1999

PubMed Abstract: 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.

PubMed: 10196134
DOI: 10.1074/jbc.274.16.10673

Experimental method

X-RAY DIFFRACTION (2.3 Å)