5MAP

X-ray generated oxyferrous complex of DtpA from Streptomyces lividans

Summary for 5MAP

• Entry DOI: 10.2210/pdb5map/pdb
• Descriptor: DtpA, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total)
• Functional Keywords: peroxidase radiolysis oxygen dye-type, oxidoreductase
• Biological source: Streptomyces lividans TK24
• Total number of polymer chains: 2
• Total formula weight: 82345.51

Authors

Moreno Chicano, T.,Chaplin, A.K.,Worrall, J.A.R.,Strange, R.W.,Hough, M.A. (deposition date: 2016-11-04, release date: 2017-05-10, Last modification date: 2024-01-17)

Primary citation

Kekilli, D.,Moreno-Chicano, T.,Chaplin, A.K.,Horrell, S.,Dworkowski, F.S.N.,Worrall, J.A.R.,Strange, R.W.,Hough, M.A.
Photoreduction and validation of haem-ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction.
IUCrJ, 4:263-270, 2017

PubMed Abstract: Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into redox, ligand and spin states to complement the information gained from the electron-density maps. The correct assignment of crystal structures to the correct protein redox and ligand states is essential to avoid the misinterpretation of structural data. This is a particular concern for haem proteins, which can occupy a wide range of redox states and are exquisitely sensitive to becoming reduced by solvated electrons generated from interactions of X-rays with water molecules in the crystal. Here, single-crystal spectroscopic fingerprinting has been applied to investigate the laser photoreduction of ferric haem in cytochrome '. Furthermore, X-ray-driven generation of haem intermediates in crystals of the dye-decolourizing-type peroxidase A (DtpA) from is described.

PubMed: 28512573
DOI: 10.1107/S2052252517002159

Experimental method

X-RAY DIFFRACTION (1.49 Å)