1AKK

SOLUTION STRUCTURE OF OXIDIZED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1AKK

• Entry DOI: 10.2210/pdb1akk/pdb
• NMR Information: BMRB: 5660
• Descriptor: CYTOCHROME C, HEME C (2 entities in total)
• Functional Keywords: electron transport, cytochrome c
• Biological source: Equus caballus (horse)
• Cellular location: Mitochondrion matrix: P00004
• Total number of polymer chains: 1
• Total formula weight: 12344.10

Authors

Banci, L.,Bertini, I.,Gray, H.B.,Luchinat, C.,Reddig, T.,Rosato, A.,Turano, P. (deposition date: 1997-05-22, release date: 1997-09-17, Last modification date: 2024-11-20)

Primary citation

Banci, L.,Bertini, I.,Gray, H.B.,Luchinat, C.,Reddig, T.,Rosato, A.,Turano, P.
Solution structure of oxidized horse heart cytochrome c.
Biochemistry, 36:9867-9877, 1997

PubMed Abstract: The solution structure of oxidized horse heart cytochrome c was obtained at pH 7.0 in 100 mM phosphate buffer from 2278 NOEs and 241 pseudocontact shift constraints. The final structure was refined through restrained energy minimization. A 35-member family, with RMSD values with respect to the average structure of 0.70 +/- 0.11 A and 1.21 +/- 0.14 A for the backbone and all heavy atoms, respectively, and with an average penalty function of 130 +/- 4.0 kJ/mol and 84 +/- 3.7 kJ/mol for NOE and pseudocontact shift constraints, respectively (corresponding to a target function of 0.9 A2 and 0.2 A2), was obtained. The solution structure is somewhat different from that recently reported (Qi et al., 1996) and appears to be similar to the X-ray structure of the same oxidation state (Bushnell et al., 1990). A noticeable difference is a rotation of 17 +/- 8 degrees of the imidazole plane between solid and solution structure. Detailed and accurate structural determinations are important within the frame of the current debate of the structural rearrangements occurring upon oxidation or reduction. From the obtained magnetic susceptibility tensor a separation of the hyperfine shifts into their contact and pseudocontact contributions is derived and compared to that of the analogous isoenzyme from S. cerevisiae and to previous results.

PubMed: 9245419
DOI: 10.1021/bi970724w

Experimental method

SOLUTION NMR