期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 279, 期 43, 页码 45185-45193出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M405013200
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资金
- NHLBI NIH HHS [R01 HL052622-07, R01 HL062244, R01 HL052622, R01 HL062244-06, R01 HL062244-05A1, R01 HL052622-08, HL52622] Funding Source: Medline
- NIAID NIH HHS [R01 AI050050, AI50050] Funding Source: Medline
- NIGMS NIH HHS [R01 GM038060, R01 GM038060-17, R01 GM038060-16A2] Funding Source: Medline
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 Angstrom 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 Gln(255) and Lys(368) 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.
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