6ZZN

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

Summary for 6ZZN

• Entry DOI: 10.2210/pdb6zzn/pdb
• Descriptor: Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex, ACETATE ION, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: bckdh, acyltransferase, lipoamide, mycobacterium, tuberculosis, coa, transferase
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 1
• Total formula weight: 24891.65

Authors

Vilela, P.,Bellinzoni, M. (deposition date: 2020-08-04, release date: 2021-08-18, Last modification date: 2024-01-31)

Primary citation

Bruch, E.M.,Vilela, P.,Yang, L.,Boyko, A.,Lexa-Sapart, N.,Raynal, B.,Alzari, P.M.,Bellinzoni, M.
Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: α-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 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.

PubMed: 34819376
DOI: 10.1073/pnas.2112107118

Experimental method

X-RAY DIFFRACTION (1.5 Å)