6zzl

Crystal structure of the catalytic domain plus N-terminal linker of the acetyltransferase AceF (E2p) from Corynebacterium glutamicum.

spinqualitylabelsall models 6zzl, resolution 2.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zzl is a 3 chain structure with sequence from Corgl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, PO4 Gene: aceF, sucB, Cgl2207, cg2421 (CORGL) Activity: Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ODP2_CORGL] Is essential for both 2-oxoglutarate dehydrogenase (ODH) and pyruvate dehydrogenase (PDH) activities, but AceF has exclusively transacetylase (and no transsuccinylase) activity. The lipoyl residues required for ODH activity are likely provided by AceF. 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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