The crystal structure of XC1258 from Xanthomonas campestris: A putative procaryotic Nit protein with an arsenic adduct in the active site

Proteins: Structure, Function and Genetics

Volumn 69, Issue 3, 2007, Pages 665-671

  Chin, Ko Hsin ^a   Tsai, Ying Der ^a   Chan, Nei Li ^a   Huang, Kai Fa ^b   Wang, Andrew H J ^b,c   Chou, Shan Ho ^a  

^a NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^b ACADEMIA SINICA   (Taiwan)

^c INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

Author keywords

Arsenic adduct; Nitrilase; Plant pathogen; X ray diffraction; Xanthomonas campestris

Indexed keywords

BACTERIAL PROTEIN; NITRILASE; PROTEIN NIT; PROTEIN XC1258; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; XANTHOMONAS CAMPESTRIS;

AMINO ACID SEQUENCE; AMINOHYDROLASES; ARSENICALS; BACTERIAL PROTEINS; BINDING SITES; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; XANTHOMONAS CAMPESTRIS;

PROKARYOTA; XANTHOMONAS CAMPESTRIS;

EID: 35448960463     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21501     Document Type: Article

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