1IYV

LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, 29 STRUCTURES

1IYV の概要

• エントリーDOI: 10.2210/pdb1iyv/pdb
• 分子名称: DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX (1 entity in total)
• 機能のキーワード: glycolysis, transferase, acyltransferase, lipoyl
• 由来する生物種: Azotobacter vinelandii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8173.40

構造登録者

Berg, A.,Vervoort, J.,De Kok, A. (登録日: 1996-09-25, 公開日: 1997-03-12, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

SOLUTION NMR