1T8T

Crystal Structure of human 3-O-Sulfotransferase-3 with bound PAP

1T8T の概要

• エントリーDOI: 10.2210/pdb1t8t/pdb
• 関連するPDBエントリー: 1BFB 1HY3 1S6T
• 分子名称: heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1, ADENOSINE-3'-5'-DIPHOSPHATE, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: alpha-beta motif, substrate-binding cleft, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus membrane ; Single-pass type II membrane protein : Q9Y662
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63190.19

構造登録者

Moon, A.F.,Edavettal, S.C.,Krahn, J.M.,Munoz, E.M.,Negishi, M.,Linhardt, R.J.,Liu, J.,Pedersen, L.C. (登録日: 2004-05-13, 公開日: 2004-08-31, 最終更新日: 2024-11-20)

主引用文献

Moon, A.F.,Edavettal, S.C.,Krahn, J.M.,Munoz, E.M.,Negishi, M.,Linhardt, R.J.,Liu, J.,Pedersen, L.C.
Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1
J.Biol.Chem., 279:45185-45193, 2004

PubMed Abstract: Heparan sulfate (HS) plays essential roles in assisting herpes simplex virus infection and other biological processes. The biosynthesis of HS includes numerous specialized sulfotransferases that generate a variety of sulfated saccharide sequences, conferring the selectivity of biological functions of HS. We report a structural study of human HS 3-O-sulfotransferase isoform 3 (3-OST-3), a key sulfotransferase that transfers a sulfuryl group to a specific glucosamine in HS generating an entry receptor for herpes simplex virus 1. We have obtained the crystal structure of 3-OST-3 at 1.95 A in a ternary complex with 3'-phosphoadenosine 5'-phosphate and a tetrasaccharide substrate. Mutational analyses were also performed on the residues involved in the binding of the substrate. Residues Gln255 and Lys368 are essential for the sulfotransferase activity and lie within hydrogen bonding distances to the carboxyl and sulfo groups of the uronic acid unit. These residues participate in the substrate recognition of 3-OST-3. This structure provides atomic level evidence for delineating the substrate recognition and catalytic mechanism for 3-OST-3.

PubMed: 15304505
DOI: 10.1074/jbc.M405013200

実験手法

X-RAY DIFFRACTION (1.85 Å)