Open AccessCrystallization and preliminary crystallographic analysis of cg Hle, a homoserine acetyltransferase homologue, from Corynebacterium glutamicum
Author(s) -
Tölzer Christine,
Pal Sonia,
Watzlawick Hildegard,
Altenbuchner Josef,
Niefind Karsten
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108039146
Subject(s) - corynebacterium glutamicum , orthorhombic crystal system , crystallization , monoclinic crystal system , homoserine , crystallography , crystal (programming language) , methionine , corynebacterium , transferase , biosynthesis , homology (biology) , trigonal crystal system , chemistry , stereochemistry , crystal structure , enzyme , biochemistry , gene , biology , amino acid , bacteria , organic chemistry , genetics , quorum sensing , virulence , computer science , programming language
Cg Hle is an enzyme that is encoded by gene cg0961 from Corynebacterium glutamicum . The physiological function of cg Hle is so far unclear. Bioinformatic annotations based on sequence homology indicated that cg Hle may be an acetyl‐CoA:homoserine acetyl transferase and as such may be involved in methionine biosynthesis, but recent evidence has shown that it is an esterase that catalyzes the hydrolysis of acetyl esters. Here, the crystallization of cg Hle in two orthorhombic crystal forms, a trigonal crystal form and a monoclinic crystal form is described. The trigonal crystals have a solvent content of 83.7%, which is one of the highest solvent contents ever found for protein crystals. One of the orthorhombic crystals diffracted X‐rays to at least 1.2 Å resolution.