Tolzer_2009_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_65_34

Reference

Title : Crystallization and preliminary crystallographic analysis of cgHle, a homoserine acetyltransferase homologue, from Corynebacterium glutamicum - Tolzer_2009_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_65_34
Author(s) : Tolzer C , Pal S , Watzlawick H , Altenbuchner J , Niefind K
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 65 :34 , 2009
Abstract :

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.

PubMedSearch : Tolzer_2009_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_65_34
PubMedID: 19153452
Gene_locus related to this paper: corgl-CGL0839

Related information

Gene_locus corgl-CGL0839

Citations formats

Tolzer C, Pal S, Watzlawick H, Altenbuchner J, Niefind K (2009)
Crystallization and preliminary crystallographic analysis of cgHle, a homoserine acetyltransferase homologue, from Corynebacterium glutamicum
Acta Crystallographica Sect F Struct Biol Cryst Commun 65 :34

Tolzer C, Pal S, Watzlawick H, Altenbuchner J, Niefind K (2009)
Acta Crystallographica Sect F Struct Biol Cryst Commun 65 :34