Open AccessCloning, crystallization and preliminary X‐ray study of XC1258, a CN‐hydrolase superfamily protein from Xanthomonas campestris
Author(s) -
Tsai YingDer,
Chin KoHsin,
Gao Fei Philip,
Shr HuiLin,
Lyu PingChiang,
Wang Andrew H.J.,
Chou ShanHo
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106035433
Subject(s) - hydrolase , xanthomonas campestris , cloning (programming) , biochemistry , peptide sequence , chemistry , biology , stereochemistry , enzyme , gene , computer science , programming language
CN‐hydrolase superfamily proteins are involved in a wide variety of non‐peptide carbon–nitrogen hydrolysis reactions, producing some important natural products such as auxin, biotin, precursors of antibiotics etc . These reactions all involve attack on a cyano or carbonyl carbon by a conserved novel catalytic triad Glu‐Lys‐Cys through a thiol acylenzyme intermediate. However, classification into the CN‐hydrolase superfamily based on sequence similarity alone is not straightforward and further structural data are necessary to improve this categorization. Here, the cloning, expression, crystallization and preliminary X‐ray analysis of XC1258, a CN‐hydrolase superfamily protein from the plant pathogen Xanthomonas campestris (Xcc), are reported. The SeMet‐substituted XC1258 crystals diffracted to a resolution of 1.73 Å. They are orthorhombic and belong to space group P 2 1 2 1 2, with unit‐cell parameters a = 143.8, b = 154.63, c = 51.3 Å, respectively.