7B9K

Cryo-EM structure of the dihydrolipoyl transacetylase cubic core of the E. coli pyruvate dehydrogenase complex including lipoyl domains

Summary for 7B9K

• Entry DOI: 10.2210/pdb7b9k/pdb
• EMDB information: 12104
• Descriptor: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (1 entity in total)
• Functional Keywords: multienzyme complexes, oxoacid dehydrogenase complexes, lipoic acid, dihydrolipoyllysine, transferase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 24
• Total formula weight: 1592716.87

Authors

Skerlova, J.,Stenmark, P. (deposition date: 2020-12-14, release date: 2021-08-11, Last modification date: 2021-10-06)

Primary citation

Skerlova, J.,Berndtsson, J.,Nolte, H.,Ott, M.,Stenmark, P.
Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion.
Nat Commun, 12:5277-5277, 2021

PubMed Abstract: The pyruvate dehydrogenase complex (PDHc) links glycolysis to the citric acid cycle by converting pyruvate into acetyl-coenzyme A. PDHc encompasses three enzymatically active subunits, namely pyruvate dehydrogenase, dihydrolipoyl transacetylase, and dihydrolipoyl dehydrogenase. Dihydrolipoyl transacetylase is a multidomain protein comprising a varying number of lipoyl domains, a peripheral subunit-binding domain, and a catalytic domain. It forms the structural core of the complex, provides binding sites for the other enzymes, and shuffles reaction intermediates between the active sites through covalently bound lipoyl domains. The molecular mechanism by which this shuttling occurs has remained elusive. Here, we report a cryo-EM reconstruction of the native E. coli dihydrolipoyl transacetylase core in a resting state. This structure provides molecular details of the assembly of the core and reveals how the lipoyl domains interact with the core at the active site.

PubMed: 34489474
DOI: 10.1038/s41467-021-25570-y

Experimental method

ELECTRON MICROSCOPY (3.16 Å)