Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis.

Journal of molecular biology - 5 Jul 2002

Cohen-Gonsaud Martin, Ducasse Stéphanie, Hoh Francois, Zerbib Didier, Labesse Gilles, Quemard Annaïk

Abstract excerpt

The fatty acid elongation system FAS-II is involved in the biosynthesis of mycolic acids, which are major and specific long-chain fatty acids of the cell envelope of Mycobacterium tuberculosis and other mycobacteria, including Mycobacterium smegmatis. The protein MabA, also named FabG1, has been shown recently to be part of FAS-II and to catalyse the NADPH-specific reduction of long chain beta-ketoacyl...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alcohol Oxidoreductases
Share to Cross-Linking Reagents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fatty Acids

Share to Mycobacterium tuberculosis

Share to Protein Folding

Share to Scattering, Radiation

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 12079383
DOI: 10.1016/S0022-2836(02)00463-1

Genes

FAS

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis.PMID 12079383Read ↗

Ligand-induced fit in mycobacterial MabA: the sequence-specific C-terminus locks the conformational change.Semantic proximity Read ↗

The Mycobacterium Tuberculosis FAS-II Dehydratases and Methyltransferases Define the Specificity of the Mycolic Acid Elongation ComplexesSemantic proximity Read ↗

Role of Serine140 in the mode of action of Mycobacterium tuberculosis β-ketoacyl-ACP Reductase (MabA).Semantic proximity Read ↗

Protein–protein interactions within the Fatty Acid Synthase‐II system of <i>Mycobacterium tuberculosis</i> are essential for mycobacterial viabilitySemantic proximity Read ↗

The Molecular Genetics of Mycolic Acid BiosynthesisSemantic proximity Read ↗

Characterization of a beta-hydroxybutyryl-CoA dehydrogenase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolutionSemantic proximity Read ↗

Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II.Semantic proximity Read ↗

Role of long-chain acyl-CoAs in the regulation of mycolic acid biosynthesis in mycobacteria.Semantic proximity Read ↗

HadD, a novel fatty acid synthase type II protein, is essential for alpha- and epoxy-mycolic acid biosynthesis and mycobacterial fitnessSemantic proximity Read ↗

Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.Semantic proximity Read ↗

Molecular modeling studies of Fatty acyl-CoA synthetase (FadD13) from Mycobacterium tuberculosis--a potential target for the development of antitubercular drugs.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.