Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site

Structure

Volumn 8, Issue 5, 2000, Pages 505-514

  Walsh, Martin A ^a,f   Otwinowski, Zbyszek ^b   Perrakis, Anatassis ^c   Anderson, Paul M ^d   Joachimiak, Andrzej ^a,e  

^a ARGONNE NATIONAL LABORATORY   (United States)

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

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^d UNIVERSITY OF MINNESOTA DULUTH   (United States)

^e NORTHWESTERN UNIVERSITY   (United States)

^f IRBM   (Italy)

Author keywords

Active site; Cyanase; Decamer structure; MAD phasing; Monoanion and dianion inhibitors; Synchrotron radiation

Indexed keywords

BACTERIAL ENZYME; BICARBONATE; CYANIC ACID;

AMINO ACID SEQUENCE; ARTICLE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBUNIT; ENZYME SYNTHESIS; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE HOMOLOGY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034657184     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00134-9     Document Type: Article

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