6AIR
High resolution structure of perdeuterated high-potential iron-sulfur protein
Summary for 6AIR
| Entry DOI | 10.2210/pdb6air/pdb |
| Descriptor | High-potential iron-sulfur protein, IRON/SULFUR CLUSTER, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | iron-sulfur protein, metal-binding protein, metal binding protein |
| Biological source | Thermochromatium tepidum (Chromatium tepidum) |
| Total number of polymer chains | 1 |
| Total formula weight | 9809.99 |
| Authors | Hanazono, Y.,Takeda, K.,Miki, K. (deposition date: 2018-08-24, release date: 2019-08-21, Last modification date: 2023-11-22) |
| Primary citation | Hanazono, Y.,Takeda, K.,Miki, K. Characterization of perdeuterated high-potential iron-sulfur protein with high-resolution X-ray crystallography. Proteins, 88:251-259, 2020 Cited by PubMed Abstract: Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high-resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X-ray structure of perdeuterated high-potential iron-sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high-resolution neutron crystallography. PubMed: 31365157DOI: 10.1002/prot.25793 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.85 Å) |
Structure validation
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