Crystallization and preliminary crystallographic analysis of cgHle, a homoserine acetyltransferase homologue, from Corynebacterium glutamicum.
CgHle is an enzyme that is encoded by gene cg0961 from Corynebacterium glutamicum. The physiological function of cgHle is so far unclear. Bioinformatic annotations based on sequence homology indicated that cgHle 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 cgHle 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 A resolution.
Tölzer
Christine
C
Universität zu Köln, Department für Chemie, Institut für Biochemie, Köln, Germany.
Pal
Sonia
S
Watzlawick
Hildegard
H
Altenbuchner
Josef
J
Niefind
Karsten
K
D000123:Acetyltransferases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D002850:Chromatography, Gel; D048230:Corynebacterium glutamicum / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D015964:Gene Expression Regulation, Bacterial; D006868:Hydrolysis; D011994:Recombinant Proteins / Q000737:chemistry; D012997:Solvents / Q000737:chemistry
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012997:Solvents; D000123:Acetyltransferases; C021369:homoserine O-acetyltransferase