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4XVA

Crystal structure of wild type cytochrome c peroxidase

Summary for 4XVA
Entry DOI10.2210/pdb4xva/pdb
Related4XV4 4XV5 4XV6 4XV7 4XV8 4XVA
DescriptorCytochrome c peroxidase, mitochondrial, PROTOPORPHYRIN IX CONTAINING FE, BENZIMIDAZOLE, ... (4 entities in total)
Functional Keywordsmodel system, flexibility, thermodynamics, cryptic site, transient protein sites, ligand binding, oxidoreductase
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Total number of polymer chains4
Total formula weight136700.90
Authors
Fischer, M.,Fraser, J.S. (deposition date: 2015-01-26, release date: 2015-02-25, Last modification date: 2024-02-28)
Primary citationFischer, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.66 Å)
Structure validation

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