Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal β-sheet and the fingerprint region

Proteins: Structure, Function and Genetics

Volumn 65, Issue 4, 2006, Pages 1021-1031

  Ouyang, Nan ^a   Gao, Yong Guang ^b   Hu, Hong Yu ^b   Xia, Zong Xiang ^a  

^a SHANGHAI INSTITUTE OF ORGANIC CHEMISTRY   (China)

^b INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

Circular dichroism; Cis proline; Conformational change; Crystal structure; E. coli cytochrome c maturation protein; Fingerprint region; Mutant; N terminal sheet; Redox potential; Thiol: disulfide oxidoreductase

Indexed keywords

ALANINE; ARGININE; BACTERIAL PROTEIN; CIS ACTING ELEMENT; CYSTEINE; CYTOCHROME C; CYTOCHROME C MATURATION PROTEIN; DISULFIDE; GLUTAMINE; MUTANT PROTEIN; NITROGEN; OXIDOREDUCTASE; OXYGEN; PERIPLASMIC PROTEIN; PROLINE; PROTEIN DSBE; SOLVENT; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DNA FINGERPRINTING; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GENE DELETION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); PROTEIN FOLDING; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

ESCHERICHIA COLI;

EID: 33751114414     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21184     Document Type: Article

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