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M405013200v1
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Papers In Press, published online ahead of print August 10, 2004
J. Biol. Chem, 10.1074/jbc.M405013200
Submitted on May 5, 2004
Revised on August 3, 2004
Accepted on August 10, 2004

Structural analysis of the sulfotransferase (3-OST-3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1

Andrea F. Moon, Suzanne C. Edavettal, Joe M. Krahn, Eva M. Munoz, Masahiko Negishi, Robert J. Linhardt, Jian Liu, and Lars C. Pedersen

Medicinal Chemistry and Natrual Products, University of North Carolina, Chapel Hill, NC 27599

Corresponding Author: jian_liu{at}unc.edu

Summary 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 Å 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 Q255 and K368 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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