1IYU

LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1IYU

• Entry DOI: 10.2210/pdb1iyu/pdb
• Descriptor: DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX (1 entity in total)
• Functional Keywords: glycolysis, transferase, acyltransferase, lipoyl
• Biological source: Azotobacter vinelandii
• Total number of polymer chains: 1
• Total formula weight: 8173.40

Authors

Berg, A.,Vervoort, J.,De Kok, A. (deposition date: 1996-09-25, release date: 1997-03-12, Last modification date: 2024-05-22)

Primary citation

Berg, A.,Vervoort, J.,de Kok, A.
Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
Eur.J.Biochem., 244:352-360, 1997

PubMed Abstract: The three-dimensional structure of the N-terminal lipoyl domain of the acetyltransferase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii has been determined using heteronuclear multidimensional NMR spectroscopy and dynamical simulated annealing. The structure is compared with the solution structure of the lipoyl domain of the A. vinelandii 2-oxoglutarate dehydrogenase complex. The overall fold of the two structures, described as a beta-barrel-sandwich hybrid, is very similar. This agrees well with the high similarity of NMR-derived parameters, e.g. chemical shifts, between the two lipoyl domains. The main structural differences between the two lipoyl domains occur in a solvent-exposed loop close in space to the lipoylation site. Despite their high structural similarity, these lipoyl domains show a high preference for being reductively acylated by their parent 2-oxo acid dehydrogenase. Potential residues of the lipoyl domain involved in this process of molecular recognition are discussed.

PubMed: 9119000
DOI: 10.1111/j.1432-1033.1997.00352.x

Experimental method

SOLUTION NMR