The activity of Escherichia coli chaperone SurA is regulated by conformational changes involving a parvulin domain

Journal of Bacteriology

Volumn 198, Issue 6, 2016, Pages 921-929

  Soltes, Garner R ^a   Schwalm, Jaclyn ^a   Ricci, Dante P ^a,b   Silhavy, Thomas J ^a  

^a PRINCETON UNIVERSITY   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN; SURA PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; PEPTIDYLPROLYL ISOMERASE; SURA PROTEIN, E COLI;

AMINO ACID SEQUENCE; ARTICLE; BIOGENESIS; CELL VIABILITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; ESCHERICHIA COLI; ESCHERICHIA COLI O157; FIMBRIA; GAIN OF FUNCTION MUTATION; MOLECULAR WEIGHT; NONHUMAN; PARVULIN DOMAIN; PERMEABILITY BARRIER; PRIORITY JOURNAL; PROTEIN DOMAIN; SALMONELLA; SHIGELLA; UROPATHOGENIC ESCHERICHIA COLI; CHEMISTRY; DNA MUTATIONAL ANALYSIS; GENE DELETION; GENETICS; METABOLISM; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE;

BACTERIAL OUTER MEMBRANE PROTEINS; CARRIER PROTEINS; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; PEPTIDYLPROLYL ISOMERASE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION;

EID: 84960425092     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00889-15     Document Type: Article

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