The Crystal Structure of Glutamyl Endopeptidase from Bacillus intermedius Reveals a Structural Link between Zymogen Activation and Charge Compensation

Biochemistry

Volumn 43, Issue 10, 2004, Pages 2784-2791

  Meijers, Rob ^a,f   Blagova, Elena V ^b   Levdikov, Vladimir M ^b   Rudenskaya, Galina N ^c   Chestukhina, Galina G ^d   Akimkina, Tatiana V ^e   Kostrov, Sergei V ^e   Lamzin, Victor S ^a   Kuranova, Inna P ^b  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b SHUBNIKOV INSTITUTE OF CRYSTALLOGRAPHY   (Russian Federation)

^c MOSCOW STATE UNIVERSITY   (Russian Federation)

^d STATE RESEARCH INSTITUTE OF GENETICS AND SELECTION OF INDUSTRIAL MICROORGANISMS   (Russian Federation)

^e INSTITUTE OF MOLECULAR GENETICS   (Russian Federation)

^f DANA FARBER CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CATALYST ACTIVITY; CHEMICAL ACTIVATION; CHEMICAL BONDS; CRYSTAL ATOMIC STRUCTURE; ENZYMES;

PROTEIN BINDING;

BIOCHEMISTRY;

1 METHYL 2,4 PENTANEDIOL; BACTERIAL ENZYME; CHYMOTRYPSIN; ENZYME PRECURSOR; GLUTAMIC ACID; GLUTAMYL ENDOPEPTIDASE; HISTIDINE; PENTANOL; SERINE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS; BACILLUS INTERMEDIUS; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CHARGE COMPENSATION; CRYSTAL STRUCTURE; DISULFIDE BOND; ELECTRICITY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; SEQUENCE ALIGNMENT; TOPOGRAPHY;

AMINO ACID SEQUENCE; ANIONS; BACILLUS; BACTERIAL PROTEINS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; ELECTROSTATICS; ENZYME ACTIVATION; ENZYME PRECURSORS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; SERINE ENDOPEPTIDASES; STAPHYLOCOCCUS; STREPTOMYCES; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY;

BACILLUS INTERMEDIUS; BACTERIA (MICROORGANISMS);

EID: 1542297724     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035354s     Document Type: Article

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