Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism

Scientific Reports

Volumn 5, Issue , 2015, Pages

  Mendes, Vitor ^a,b   Blaszczyk, Michal ^a   Maranha, Ana ^b   Empadinhas, Nuno ^b   Blundell, Tom L ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF COIMBRA   (Portugal)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GLUCOSYLTRANSFERASE; MALTOSE; MALTOSE 1-PHOSPHATE; MALTOSYLTRANSFERASE; SUGAR PHOSPHATE;

BINDING SITE; CATALYSIS; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR MODEL; MYCOBACTERIUM; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLUCOSYLTRANSFERASES; KINETICS; MALTOSE; MODELS, MOLECULAR; MYCOBACTERIUM; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; STRUCTURE-ACTIVITY RELATIONSHIP; SUGAR PHOSPHATES;

EID: 84948667604     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep17144     Document Type: Article

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