Open AccessCloning, crystallization and preliminary X‐ray studies of XC2981 from Xanthomonas campestris , a putative CutA1 protein involved in copper‐ion homeostasis
Author(s) -
Lin ChienHung,
Chin KoHsin,
Gao Fei Philip,
Lyu PingChiang,
Shr HuiLin,
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/s1744309106039832
Subject(s) - xanthomonas campestris , crystallography , cloning (programming) , escherichia coli , crystallization , copper , chemistry , metal ions in aqueous solution , biology , xanthomonas , biochemistry , ion , gene , organic chemistry , computer science , programming language
Divalent metal ions play key roles in all living organisms, serving as cofactors for many proteins involved in a variety of electron‐transfer activities. However, copper ions are highly toxic when an excessive amount is accumulated in a cell. CutA1 is a protein found in all kingdoms of life that is believed to participate in copper‐ion tolerance in Escherichia coli , although its specific function remains unknown. Several crystal structures of multimeric CutA1 with different rotation angles and degrees of interaction between trimer interfaces have been reported. Here, the cloning, expression, crystallization and preliminary X‐ray analysis of XC2981, a possible CutA1 protein present in the plant pathogen Xanthomonas campestris , are reported. The XC2981 crystals diffracted to a resolution of 2.6 Å. They are cubic and belong to space group I 23, with unit‐cell parameters a = b = c = 130.73 Å.