Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1YNR

Crystal structure of the cytochrome c-552 from Hydrogenobacter thermophilus at 2.0 resolution

1YNR の概要
エントリーDOI10.2210/pdb1ynr/pdb
関連するPDBエントリー1AYG
分子名称Cytochrome c-552, SULFATE ION, HEME C, ... (5 entities in total)
機能のキーワードhelix, electron transport
由来する生物種Hydrogenobacter thermophilus
タンパク質・核酸の鎖数4
化学式量合計38051.65
構造登録者
Travaglini-Allocatelli, C.,Gianni, S.,Dubey, V.K.,Borgia, A.,Di Matteo, A.,Bonivento, D.,Cutruzzola, F.,Bren, K.L.,Brunori, M. (登録日: 2005-01-25, 公開日: 2005-05-17, 最終更新日: 2024-10-16)
主引用文献Travaglini-Allocatelli, C.,Gianni, S.,Dubey, V.K.,Borgia, A.,Di Matteo, A.,Bonivento, D.,Cutruzzola, F.,Bren, K.L.,Brunori, M.
An Obligatory Intermediate in the Folding Pathway of Cytochrome c552 from Hydrogenobacter thermophilus
J.Biol.Chem., 280:25729-25734, 2005
Cited by
PubMed Abstract: The folding mechanism of many proteins involves the population of partially organized structures en route to the native state. Identification and characterization of these intermediates is particularly difficult, as they are often only transiently populated and may play different mechanistic roles, being either on-pathway productive species or off-pathway kinetic traps. Following different spectroscopic probes, and employing state-of-the-art kinetic analysis, we present evidence that the folding mechanism of the thermostable cytochrome c552 from Hydrogenobacter thermophilus does involve the presence of an elusive, yet compact, on-pathway intermediate. Characterization of the folding mechanism of this cytochrome c is particularly interesting for the purpose of comparative folding studies, because H. thermophilus cytochrome c552 shares high sequence identity and structural homology with its homologue from the mesophilic bacterium Pseudomonas aeruginosa cytochrome c551, which refolds through a broad energy barrier without the accumulation of intermediates. Analysis of the folding kinetics and correlation with the three-dimensional structure add new evidence for the validity of a consensus folding mechanism in the cytochrome c family.
PubMed: 15883159
DOI: 10.1074/jbc.M502628200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1ynr
検証レポート(詳細版)ダウンロードをダウンロード

252456

件を2026-04-22に公開中

PDB statisticsPDBj update infoContact PDBjnumon