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The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum
Author(s) -
Kim Choel,
Xuong Nguyen-Huu,
Edwards Steven,
Yee Muh-Ching,
Spraggon Glen,
E. Mills Stanley
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02905-8
Subject(s) - phosphoribosyltransferase , chemistry , homology modeling , active site , enzyme , biochemistry , stereochemistry , hypoxanthine guanine phosphoribosyltransferase , mutant , gene
The structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 Å in complex with Mn 2+ ‐pyrophosphate, and at 1.9 Å without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, α and α/β, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known.