1HRQ
THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR
Summary for 1HRQ
| Entry DOI | 10.2210/pdb1hrq/pdb |
| Descriptor | HIGH POTENTIAL IRON SULFUR PROTEIN, IRON/SULFUR CLUSTER (2 entities in total) |
| Functional Keywords | electron transfer (iron-sulfur protein) |
| Biological source | Allochromatium vinosum |
| Cellular location | Periplasm: P00260 |
| Total number of polymer chains | 1 |
| Total formula weight | 9264.57 |
| Authors | Banci, L.,Bertini, I.,Dikiy, A.,Kastrau, D.H.W.,Luchinat, C.,Sompornpisut, P. (deposition date: 1995-01-17, release date: 1995-06-03, Last modification date: 2024-05-22) |
| Primary citation | Banci, L.,Bertini, I.,Dikiy, A.,Kastrau, D.H.,Luchinat, C.,Sompornpisut, P. The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Biochemistry, 34:206-219, 1995 Cited by PubMed Abstract: The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639] has been extended up to 85% of the total protein protons. Ninety percent of the nitrogens have been assigned. Then the solution structure has been obtained using as many as 1147 meaningful NOE connectivities. The protein is sizably paramagnetic even though the ground state is a singlet. Nevertheless, the final RMSD values are 0.62 and 1.19 A for the backbone and the heavy atoms, respectively. These values compare well with those for diamagnetic proteins of the same size. The solution structure is discussed in the light of the available structural information from X-ray data. PubMed: 7819198DOI: 10.1021/bi00001a025 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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