Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide

Acta Crystallographica Section F: Structural Biology Communications

Volumn 71, Issue , 2015, Pages 295-303

  Bradshaw, William J ^a,b   Roberts, April K ^b   Shone, Clifford C ^b   Acharya, K Ravi ^a  

^a University of Bath   (United Kingdom)

^b PUBLIC HEALTH ENGLAND   (United Kingdom)

Author keywords

Clostridium difficile; Cwp84; host pathogen interactions; surface layer

Indexed keywords

BACTERIA (MICROORGANISMS); CLOSTRIDIUM DIFFICILE;

BACTERIAL PROTEIN; CWP84 PROTEIN, CLOSTRIDIUM DIFFICILE; CYSTEINE PROTEINASE; PROTEIN PRECURSOR;

CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; HYDROGEN BOND; PEPTOCLOSTRIDIUM DIFFICILE; PROTEIN DEGRADATION; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; CLOSTRIDIUM DIFFICILE; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; PROTEIN PRECURSORS; PROTEOLYSIS;

EID: 84924673247     PISSN: None     EISSN: 2053230X     Source Type: Journal    
DOI: 10.1107/S2053230X15001065     Document Type: Article

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