The Rho GTPase inactivation domain in Vibrio cholerae MARTX toxin has a circularly permuted papain-like thiol protease fold

Proteins: Structure, Function and Bioinformatics

Volumn 77, Issue 2, 2009, Pages 413-419

  Pei, Jimin ^a   Grishin, Nick V ^a,b  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Autoprocessing RTX toxins; Cysteine protease domain; Homology inference; Multifunctional; Papain like fold; Rho GTPase inactivation; Shigella virulence factor IcsB; Structure prediction

Indexed keywords

CHOLERA TOXIN; CYSTEINE; HISTIDINE; MARTX TOXIN; MEMBRANE PROTEIN; PAPAIN; PROTEIN BOPA; PROTEIN ICSB; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; THIOL PROTEINASE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

ARTICLE; AUTOPHAGY; BACTERIAL VIRULENCE; BURKHOLDERIA PSEUDOMALLEI; DEPOLYMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SHIGELLA FLEXNERI; VIBRIO CHOLERAE;

ACYLTRANSFERASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BURKHOLDERIA PSEUDOMALLEI; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RHO GTP-BINDING PROTEINS; SEQUENCE ALIGNMENT; SHIGELLA FLEXNERI; VIBRIO CHOLERAE;

BACTERIA (MICROORGANISMS); BURKHOLDERIA PSEUDOMALLEI; SHIGELLA; SHIGELLA FLEXNERI; VIBRIO CHOLERAE;

EID: 70349445327     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22447     Document Type: Article

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