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TitleActinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 48, Year 2021
Publish dateNov 30, 2021
AuthorsEduardo M Bruch / Pierre Vilela / Lu Yang / Alexandra Boyko / Norik Lexa-Sapart / Bertrand Raynal / Pedro M Alzari / Marco Bellinzoni /
PubMed Abstractα-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, ...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.
External linksProc Natl Acad Sci U S A / PubMed:34819376 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.35 - 3.92 Å
Structure data

EMDB-11600:
Cubic core of the dihydrolipoamide acyltransferase (E2b) component of the branched-chain alpha-ketoacid dehydrogenase complex (BCKDH) from M. tuberculosis
Method: EM (single particle) / Resolution: 3.92 Å

PDB-6zzi:
Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p).
Method: X-RAY DIFFRACTION / Resolution: 1.932 Å

PDB-6zzj:
Crystal structure of the catalytic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p) in complex with oxidized CoA.
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-6zzk:
Crystal structure of the catalytic domain of C. glutamicum AceF (E2p) in ternary complex with CoA and dihydrolipoamide.
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-6zzl:
Crystal structure of the catalytic domain plus N-terminal linker of the acetyltransferase AceF (E2p) from Corynebacterium glutamicum.
Method: X-RAY DIFFRACTION / Resolution: 2.229 Å

PDB-6zzm:
Crystal structure of the catalytic domain of Corynebacterium mustelae predicted acetyltransferase AceF (E2p).
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6zzn:
Crystal structure of the cubic catalytic core of the Mycobacterium tuberculosis branched-chain alphaketoacid acyltransferase component (E2b).
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CAO:
OXIDIZED COENZYME A

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-COA:
COENZYME A

ChemComp-LPM:
6,8-DIMERCAPTO-OCTANOIC ACID AMIDE

ChemComp-GOL:
GLYCEROL

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ACT:
ACETATE ION

ChemComp-IMD:
IMIDAZOLE

Source
  • mycobacterium tuberculosis h37rv (bacteria)
  • corynebacterium glutamicum (strain atcc 13032 / dsm 20300 / jcm 1318 / lmg 3730 / ncimb 10025) (bacteria)
  • corynebacterium glutamicum atcc 13032 (bacteria)
  • corynebacterium mustelae (bacteria)
KeywordsTRANSFERASE / PDH / ODH / acetyltransferase / lipoamide / corynebacterium / CoA / BCKDH / acyltransferase / mycobacterium / tuberculosis

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