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Article

Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.

Acta crystallographica. Section D, Biological crystallography - 1 Aug 2007

Poncet-Montange Guillaume, Ducasse-Cabanot Stephanie, Quemard Annaick, Labesse Gilles, Cohen-Gonsaud Martin

Abstract excerpt

The MabA protein from Mycobacterium tuberculosis is a validated drug target. Previous structural studies of this protein showed dynamic behaviour in the catalytic site and described motion between an open 'active' holo form (with NADP) and a closed 'inactive' apo form (without NADP). Here, a mutation (G139A) is reported that leads to complete protein inactivation and freezes the catalytic site into its closed...

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Identifiers

PMID: 17642518
DOI: 10.1107/S0907444907024158

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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