The structure of PhaZ7 at atomic (1.2 Å) resolution reveals details of the active site and suggests a substrate-binding mode

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 66, Issue 6, 2010, Pages 648-654

  Wakadkar, Sachin ^a   Hermawan, Siska ^b   Jendrossek, Dieter ^b   Papageorgiou, Anastassios C ^a  

^a UNIVERSITY OF TURKU   (Finland)

^b UNIVERSITY OF STUTTGART   (Germany)

Author keywords

Biodegradation; Biopolymers; Catalytic mechanism; Catalytic triad; Hydrolase fold; Inhibitor binding; Oxyanion hole

Indexed keywords

BACTERIAL PROTEIN; CARBOXYLESTERASE; PHAZ7 PROTEIN, PAUCIMONAS LEMOIGNEI; SULFUR DIOXIDE;

ARTICLE; BURKHOLDERIACEAE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; METABOLISM; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; BURKHOLDERIACEAE; CARBOXYLIC ESTER HYDROLASES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY; SULFUR DIOXIDE;

BACTERIA (MICROORGANISMS); PAUCIMONAS LEMOIGNEI;

EID: 77953171895     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S174430911001434X     Document Type: Article

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