The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker

Structure

Volumn 8, Issue 4, 2000, Pages 429-440

  Vetting, Matthew W ^a   Ohlendorf, Douglas H ^a  

^a Department of Biochemistry   (United States)

Author keywords

Aromatic catabolism; Intradiol dioxygenase; Ligand dissociation; Metalloenzyme; Phospholipid

Indexed keywords

CATECHOL 1,2 DIOXYGENASE; METALLOPROTEIN; PHOSPHOLIPID; DIOXYGENASE; ENZYME INHIBITOR; MERCURIC CHLORIDE; OXYGENASE; PROTOCATECHUATE 3,4 DIOXYGENASE;

ARTICLE; CATABOLISM; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; ACINETOBACTER; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DRUG ANTAGONISM; ENZYMOLOGY; METABOLISM; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ACINETOBACTER SP.; ESCHERICHIA COLI;

ACINETOBACTER; BINDING SITES; CATALYTIC DOMAIN; CATECHOL 1,2-DIOXYGENASE; CRYSTALLOGRAPHY, X-RAY; DIOXYGENASES; ENZYME INHIBITORS; MERCURIC CHLORIDE; MODELS, MOLECULAR; OXYGENASES; PHOSPHOLIPIDS; PROTEIN CONFORMATION; PROTOCATECHUATE-3,4-DIOXYGENASE;

EID: 0034654852     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00122-2     Document Type: Article

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