1SS1

STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES

1SS1 の概要

• エントリーDOI: 10.2210/pdb1ss1/pdb
• 分子名称: Immunoglobulin G binding protein A (1 entity in total)
• 機能のキーワード: immunoglobulin-binding protein, three-helical bundle, immune system
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): P38507
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6945.58

構造登録者

Sato, S.,Religa, T.L.,Daggett, V.,Fersht, A.R. (登録日: 2004-03-23, 公開日: 2004-04-06, 最終更新日: 2024-05-22)

主引用文献

Sato, S.,Religa, T.L.,Daggett, V.,Fersht, A.R.
From The Cover: Testing protein-folding simulations by experiment: B domain of protein A.
Proc.Natl.Acad.Sci.USA, 101:6952-6956, 2004

PubMed Abstract: We have assessed the published predictions of the pathway of folding of the B domain of protein A, the pathway most studied by computer simulation. We analyzed the transition state for folding of the three-helix bundle protein, by using experimental Phi values on some 70 suitable mutants. Surprisingly, the third helix, which has the most stable alpha-helical structure as a peptide fragment, is poorly formed in the transition state, especially at its C terminus. The protein folds around a nearly fully formed central helix, which is stabilized by extensive hydrophobic side chain interactions. The turn connecting the poorly structured first helix to the central helix is unstructured, but the turn connecting the central helix to the third is in the process of being formed as the N-terminal region of the third helix begins to coalesce. The transition state is inconsistent with a classical framework mechanism and is closer to nucleation-condensation. None of the published atomistic simulations are fully consistent with the experimental picture although many capture important features. There is a continuing need for combining simulation with experiment to describe folding pathways, and of continued testing to improve predictive methods.

PubMed: 15069202
DOI: 10.1073/pnas.0401396101

実験手法

SOLUTION NMR