Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM

Acta Crystallographica Section D: Biological Crystallography

Volumn 64, Issue 2, 2008, Pages 178-188

  Alahuhta, Markus ^a   Casteleijn, Marco G ^a   Neubauer, Peter ^a   Wierenga, Rik K ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

Hinge; Loop 6; Monomeric TIM; Structural plasticity

Indexed keywords

TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYME STABILITY; GENETICS; KINETICS; METABOLISM; METHODOLOGY; MUTATION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TRIOSE-PHOSPHATE ISOMERASE;

EID: 38549151788     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444907059021     Document Type: Article

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