2K7V

Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form

2K7V の概要

• エントリーDOI: 10.2210/pdb2k7v/pdb
• NMR情報: BMRB: 15931
• 分子名称: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (1 entity in total)
• 機能のキーワード: misfolded dimer, acyltransferase, glycolysis, lipoyl, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17774.65

構造登録者

Stott, K.M.,Yusof, A.M.,Perham, R.N.,Jones, D.D. (登録日: 2008-08-27, 公開日: 2009-09-15, 最終更新日: 2024-05-08)

主引用文献

Stott, K.M.,Yusof, A.M.,Perham, R.N.,Jones, D.D.
A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.
Structure, 17:1117-1127, 2009

PubMed Abstract: A prominent surface loop links the first two beta strands of the lipoyl domain (E2plip) from the pyruvate dehydrogenase multienzyme complex of Escherichia coli. We show here that shortening this loop by two residues generates a protein that populates two structurally distinct stable conformers: an active, native-like monomer (HM) and a functionally compromised misfolded dimer (LM). Conversion of LM to HM was observed after exposure to temperatures above 50 degrees C. Removal of two additional residues from the loop caused the protein to adopt exclusively the misfolded conformation. Detailed NMR structural studies of the misfolded dimer reveal that the N-terminal half of the domain was unfolded and dynamic, whereas the C-terminal halves of two monomers had associated to form a structure with two-fold symmetry and a topology mimicking that of the folded monomer. The surface loop is therefore a hitherto unsuspected determinant in the folding process that leads to a functional protein.

PubMed: 19679089
DOI: 10.1016/j.str.2009.07.001

実験手法

SOLUTION NMR