PMID- 10196134
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 16
DP  - 1999 Apr 16
TI  - Crystal structure of the sulfotransferase domain of human heparan sulfate
      N-deacetylase/ N-sulfotransferase 1.
PG  - 10673-6
AB  - 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.
FAU - Kakuta, Y
AU  - Kakuta Y
AD  - Pharmacogenetics Section, Laboratory of Reproductive and Developmental
      Toxicology, NIEHS, National Institutes of Health, Research Triangle Park, North
      Carolina 27709, USA.
FAU - Sueyoshi, T
AU  - Sueyoshi T
FAU - Negishi, M
AU  - Negishi M
FAU - Pedersen, L C
AU  - Pedersen LC
LA  - eng
SI  - PDB/1NST
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 2.8.2.- (Sulfotransferases)
RN  - EC 2.8.2.8 (heparitin sulfotransferase)
RN  - EC 3.5.- (Amidohydrolases)
SB  - IM
MH  - Amidohydrolases/*chemistry/metabolism
MH  - Catalytic Domain
MH  - Crystallography, X-Ray
MH  - Humans
MH  - Models, Molecular
MH  - Substrate Specificity
MH  - Sulfotransferases/*chemistry/metabolism
EDAT- 1999/04/10 00:00
MHDA- 1999/04/10 00:01
CRDT- 1999/04/10 00:00
PHST- 1999/04/10 00:00 [pubmed]
PHST- 1999/04/10 00:01 [medline]
PHST- 1999/04/10 00:00 [entrez]
AID - 10.1074/jbc.274.16.10673 [doi]
AID - S0021-9258(19)73553-4 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 16;274(16):10673-6. doi: 10.1074/jbc.274.16.10673.