Conserved Structural Elements in Glutathione Transferase Homologues Encoded in the Genome of Escherichia coli

Proteins: Structure, Function and Genetics

Volumn 53, Issue 4, 2003, Pages 777-782

  Rife, Chris L ^a   Parsons, James F ^a   Xiao, Gaoyi ^b   Gilliland, Gary L ^b   Armstrong, Richard N ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

Author keywords

Consensus sequence; Domain structure; Glutathionylspermidine; Selenium; Stringent starvation protein; X ray crystallography

Indexed keywords

GLUTATHIONE TRANSFERASE; THIOREDOXIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; BACTERIAL GENOME; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GENE SEGREGATION; GENE STRUCTURE; GENETIC CODE; GENETIC CONSERVATION; GST GENE; HYDROPHOBICITY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENOME, BACTERIAL; GLUTATHIONE TRANSFERASE; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI;

EID: 0344118144     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10452     Document Type: Article

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