Three clusters of conformational states in P450cam reveal a multistep pathway for closing of the substrate access channel

Biochemistry

Volumn 50, Issue 5, 2011, Pages 693-703

  Lee, Young Tae ^a   Glazer, Edith C ^a,b   Wilson, Richard F ^a   Stout, C David ^a   Goodin, David B ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CONFORMATIONAL CHANGE; CONFORMATIONAL PLASTICITY; CONFORMATIONAL SELECTION; CONFORMATIONAL STATE; CYTOCHROME P450; MULTI-STEP; OPEN CONFORMATION; PROTEIN CONFORMATION; SUBSTRATE BINDING; SUBSTRATE SPECIFICITY;

PRINCIPAL COMPONENT ANALYSIS;

SUBSTRATES;

CYTOCHROME P450;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PRINCIPAL COMPONENT ANALYSIS; PRIORITY JOURNAL;

BACTERIAL PROTEINS; CAMPHOR 5-MONOOXYGENASE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; PROTEIN BINDING; PROTEIN CONFORMATION; PSEUDOMONAS PUTIDA; SUBSTRATE SPECIFICITY;

EID: 79952092257     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101726d     Document Type: Article

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