4XVA

Crystal structure of wild type cytochrome c peroxidase

4XVA の概要

• エントリーDOI: 10.2210/pdb4xva/pdb
• 関連するPDBエントリー: 4XV4 4XV5 4XV6 4XV7 4XV8 4XVA
• 分子名称: Cytochrome c peroxidase, mitochondrial, PROTOPORPHYRIN IX CONTAINING FE, BENZIMIDAZOLE, ... (4 entities in total)
• 機能のキーワード: model system, flexibility, thermodynamics, cryptic site, transient protein sites, ligand binding, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 136700.90

構造登録者

Fischer, M.,Fraser, J.S. (登録日: 2015-01-26, 公開日: 2015-02-25, 最終更新日: 2024-02-28)

主引用文献

Fischer, M.,Shoichet, B.K.,Fraser, J.S.
One Crystal, Two Temperatures: Cryocooling Penalties Alter Ligand Binding to Transient Protein Sites.
Chembiochem, 16:1560-1564, 2015

PubMed Abstract: Interrogating fragment libraries by X-ray crystallography is a powerful strategy for discovering allosteric ligands for protein targets. Cryocooling of crystals should theoretically increase the fraction of occupied binding sites and decrease radiation damage. However, it might also perturb protein conformations that can be accessed at room temperature. Using data from crystals measured consecutively at room temperature and at cryogenic temperature, we found that transient binding sites could be abolished at the cryogenic temperatures employed by standard approaches. Changing the temperature at which the crystallographic data was collected could provide a deliberate perturbation to the equilibrium of protein conformations and help to visualize hidden sites with great potential to allosterically modulate protein function.

PubMed: 26032594
DOI: 10.1002/cbic.201500196

実験手法

X-RAY DIFFRACTION (2.66 Å)