(PDF) Structure ofMethylobacterium Extorquensmalyl-CoA

Structure ofMethylobacterium Extorquensmalyl-CoA Lyase: CoA-substrate Binding Correlates With Domain Shift

Acta Crystallographica Section F:Structural Biology Communications - United Kingdom

doi 10.1107/s2053230x17001029

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January 27, 2017

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International Union of Crystallography (IUCr)

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Structure ofMethylobacterium Extorquensmalyl-CoA Lyase: CoA-substrate Binding Correlates With Domain Shift

Acta Crystallographica Section F:Structural Biology Communications - United Kingdom

doi 10.1107/s2053230x17001029

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

X-Ray Structure of Pyruvate Formate-Lyase in Complex With Pyruvate and CoA

Structural Features and Domain Movements Controlling Substrate Binding and Cofactor Specificity in Class II HMG-CoA Reductase

Structural Basis for Substrate Specificity in Adenosylcobalamin-Dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases

A Nonsense Mutation in the 3-Hydroxy-3-Methylglutaryl-CoA Lyase Gene Produces Exon Skipping in Two Patients of Different Origin With 3-Hydroxy-3-Methylglutaryl-CoA Lyase Deficiency

Comparison of the Binding Affinities of Acyl-CoA-Binding Protein and Fatty-Acid-Binding Protein for Long-Chain Acyl-CoA Esters

Structure and Function of a Single-Chain, Multi-Domain Long-Chain Acyl-CoA Carboxylase

Regulation of Acetyl-coA Carboxylase: Properties of coA Activation of Acetyl-coA Carboxylase.

A Ternary Complex of Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) With Acetyl-Coenzyme a and Vanillin Gives Insights Into Substrate Specificity and Mechanism.

Binding of Activated Isoniazid With Acetyl-CoA Carboxylase From Mycobacterium Tuberculosis