6zzn

Crystal structure of the cubic catalytic core of the Mycobacterium tuberculosis branched-chain alphaketoacid acyltransferase component (E2b).

spinqualitylabelsall models 6zzn, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zzn is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: ACT, IMD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BKDC_MYCTU Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2). Publication Abstract from PubMed alpha-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, all considered to be structured around a high-molecular weight hollow core, consisting of up to 60 subunits of the acyltransferase component. We provide here evidence that Actinobacteria break the rule by possessing an acetyltranferase component reduced to its minimally active, trimeric unit, characterized by a unique C-terminal helix bearing an actinobacterial specific insertion that precludes larger protein oligomerization. This particular feature, together with the presence of an odhA gene coding for both the decarboxylase and the acyltransferase domains on the same polypetide, is spread over Actinobacteria and reflects the association of PDH and ODH into a single physical complex. Considering the central role of the pyruvate and 2-oxoglutarate nodes in central metabolism, our findings pave the way to both therapeutic and metabolic engineering applications. Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.,Bruch EM, Vilela P, Yang L, Boyko A, Lexa-Sapart N, Raynal B, Alzari PM, Bellinzoni M Proc Natl Acad Sci U S A. 2021 Nov 30;118(48). pii: 2112107118. doi:, 10.1073/pnas.2112107118. PMID:34819376 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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