Structural basis unifying diverse GTP hydrolysis mechanisms

Biochemistry

Volumn 52, Issue 6, 2013, Pages 1122-1130

  Anand, Baskaran ^a,b   Majumdar, Soneya ^a   Prakash, Balaji ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; BIOLOGICAL PROCESS; CONSTITUTIVELY ACTIVES; DIFFERENT MECHANISMS; DYNAMIN; GTP HYDROLYSIS; GTPASE-ACTIVATING PROTEIN; GTPASES; STERIC HINDRANCES; STRUCTURAL BASIS; TRANSITION STATE; UNDERLYING PRINCIPLES;

ARGININE; CATALYSIS;

HYDROLYSIS;

ARGININE; DYNAMIN; GUANOSINE TRIPHOSPHATASE; POTASSIUM ION; SODIUM ION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOLOGICAL PHENOMENA AND FUNCTIONS CONCERNING THE ENTIRE ORGANISM; CATALYSIS; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME STRUCTURE; HYDROPHILICITY; HYDROPHOBICITY; NUCLEOPHILICITY; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; STEREOSPECIFICITY;

ARGININE; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; GLUTAMINE; GTP PHOSPHOHYDROLASES; GTPASE-ACTIVATING PROTEINS; GUANOSINE TRIPHOSPHATE; HUMANS; HYDROLYSIS; MODELS, MOLECULAR; PROTEIN CONFORMATION; RAS PROTEINS;

EID: 84873633688     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3014054     Document Type: Article

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