Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase.

Acta crystallographica. Section F, Structural biology communications2018González JM, Marti-Arbona R, Chen JCH, et al.

Study designOther primary literature

SubjectUnknown

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Study design: Other primary literature
Subject: Unknown
Publication year: 2018
Source: doi.org
Abstract display: Not reproduced here
Publication status: Active
Status checked: 17 Aug 2026
Collected: 3 Aug 2026
Freshness: Current
Review stage: Automated
Record status: Published

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Abstract

cc by 以外（cc by-nc / cc by-nc-nd / NONE 等）は抄録を再掲しない。DOI/PMID へのリンクのみ表示する。

MeSH

Adenosine Diphosphate RiboseAmino Acid SequenceApoenzymesBacterial ProteinsCatalytic DomainCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionGenetic VectorsHydrogen BondingKineticsMalate DehydrogenaseMalatesMethylobacterium extorquensModels, MolecularNADOxaloacetic AcidProtein BindingProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsProtein MultimerizationProtonsRecombinant ProteinsSubstrate Specificity

DOI 10.1107/s2053230x18011809

PMID 30279311

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