7VOS
High-resolution neutron and X-ray joint refined structure of high-potential iron-sulfur protein in the oxidized state
Summary for 7VOS
| Entry DOI | 10.2210/pdb7vos/pdb |
| Descriptor | High-potential iron-sulfur protein, IRON/SULFUR CLUSTER, SULFATE ION, ... (7 entities in total) |
| Functional Keywords | iron-sulfur protein, metal binding protein |
| Biological source | Thermochromatium tepidum (Chromatium tepidum) |
| Total number of polymer chains | 1 |
| Total formula weight | 10180.47 |
| Authors | Hanazono, Y.,Hirano, Y.,Takeda, K.,Kusaka, K.,Tamada, T.,Miki, K. (deposition date: 2021-10-14, release date: 2022-06-01, Last modification date: 2024-04-03) |
| Primary citation | Hanazono, Y.,Hirano, Y.,Takeda, K.,Kusaka, K.,Tamada, T.,Miki, K. Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis. Sci Adv, 8:eabn2276-eabn2276, 2022 Cited by PubMed Abstract: The planarity of the peptide bond is important for the stability and structure formation of proteins. However, substantial distortion of peptide bonds has been reported in several high-resolution structures and computational analyses. To investigate the peptide bond planarity, including hydrogen atoms, we report a 1.2-Å resolution neutron structure of the oxidized form of high-potential iron-sulfur protein. This high-resolution neutron structure shows that the nucleus positions of the amide protons deviate from the peptide plane and shift toward the acceptors. The planarity of the H─N─C═O plane depends strongly on the pyramidalization of the nitrogen atom. Moreover, the orientation of the amide proton of Cys is different in the reduced and oxidized states, possibly because of the electron storage capacity of the iron-sulfur cluster. PubMed: 35594350DOI: 10.1126/sciadv.abn2276 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (1.2 Å) X-RAY DIFFRACTION (0.66 Å) |
Structure validation
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