Xanthomonas campestris PqqD in the pyrroloquinoline quinone biosynthesis operon adopts a novel saddle-like fold that possibly serves as a PQQ carrier

Proteins: Structure, Function and Bioinformatics

Volumn 76, Issue 4, 2009, Pages 1042-1048

  Tsai, Tung Yi ^a   Yang, Chao Yu ^a   Shih, Hui Ling ^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

Novel fold; PQQ; PqqD crystal structure; Saddle like; Xanthomonas campestris

Indexed keywords

BACTERIAL PROTEIN; GENE PRODUCT; PROTEIN PQQD; PYRROLOQUINOLINEQUINONE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; XANTHOMONAS CAMPESTRIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OPERON; PQQ COFACTOR; PROTEIN BINDING; PROTEIN FOLDING; SEQUENCE ALIGNMENT; XANTHOMONAS CAMPESTRIS;

XANTHOMONAS CAMPESTRIS;

EID: 68149098461     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22461     Document Type: Article

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