Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography
نویسندگان
چکیده
منابع مشابه
Mapping the Conformational Landscape of a Dynamic Enzyme 1 by Multitemperature and XFEL Crystallography
33 Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for 34 structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) 35 has been previously linked to its catalytic function, but the extent to which the different conformations of these 36 residues are correlated is unclear. Here we compare...
متن کاملMapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography
Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) has been previously linked to its catalytic function, but the extent to which the different conformations of these residues are correlated is unclear. Here we compare the conform...
متن کاملMapping the conformational space accessible to catechol-O-methyltransferase
Methylation catalysed by catechol-O-methyltransferase (COMT) is the main pathway of catechol neurotransmitter deactivation in the prefrontal cortex. Low levels of this class of neurotransmitters are held to be causative of diseases such as schizophrenia, depression and Parkinson's disease. Inhibition of COMT may increase neurotransmitter levels, thus offering a route for treatment. Structure-ba...
متن کاملMapping the Conformational Landscape of a Dynamic Enzyme
33 Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for 34 structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) 35 has been previously linked to its catalytic function, but the extent to which the different conformations of these 36 residues are correlated is unclear. Here we compare...
متن کاملAccessing protein conformational ensembles using room-temperature X-ray crystallography.
Modern protein crystal structures are based nearly exclusively on X-ray data collected at cryogenic temperatures (generally 100 K). The cooling process is thought to introduce little bias in the functional interpretation of structural results, because cryogenic temperatures minimally perturb the overall protein backbone fold. In contrast, here we show that flash cooling biases previously hidden...
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ژورنال
عنوان ژورنال: Structure
سال: 2016
ISSN: 0969-2126
DOI: 10.1016/j.str.2016.04.009