1YNR
Crystal structure of the cytochrome c-552 from Hydrogenobacter thermophilus at 2.0 resolution
1YNR の概要
| エントリーDOI | 10.2210/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: 15883159DOI: 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) |
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