1IT1

Solution structures of ferrocytochrome c3 from Desulfovibrio vulgaris Miyazaki F

Summary for 1IT1

• Entry DOI: 10.2210/pdb1it1/pdb
• NMR Information: BMRB: 5333
• Descriptor: cytochrome c3, HEME C (2 entities in total)
• Functional Keywords: electron transfer, tetraheme protein, electron transport
• Biological source: Desulfovibrio vulgaris str. 'Miyazaki F'
• Cellular location: Periplasm: P00132
• Total number of polymer chains: 1
• Total formula weight: 14032.29

Authors

Harada, E.,Fukuoka, Y.,Ohmura, T.,Fukunishi, A.,Kawai, G.,Fujiwara, T.,Akutsu, H. (deposition date: 2001-12-29, release date: 2002-07-10, Last modification date: 2023-12-27)

Primary citation

Harada, E.,Fukuoka, Y.,Ohmura, T.,Fukunishi, A.,Kawai, G.,Fujiwara, T.,Akutsu, H.
Redox-coupled conformational alternations in cytochrome c(3) from D. vulgaris Miyazaki F on the basis of its reduced solution structure.
J.Mol.Biol., 319:767-778, 2002

PubMed Abstract: Heteronuclear NMR spectroscopy was performed to determine the solution structure of (15)N-labeled ferrocytochrome c(3) from Desulfovibrio vulgaris Miyazaki F (DvMF). Although the folding of the reduced cytochrome c(3) in solution was similar to that of the oxidized one in the crystal structure, the region involving hemes 1 and 2 was different. The redox-coupled conformational change is consistent with the reported solution structure of D. vulgaris Hildenborough ferrocytochrome c(3), but is different from those of other cytochromes c(3). The former is homologous with DvMF cytochrome c(3) in amino acid sequence. Small displacements of hemes 1 and 2 relative to hemes 3 and 4 were observed. This observation is consistent with the unusual behavior of the 2(1)CH(3) signal of heme 3 reported previously. As shown by the (15)N relaxation parameters of the backbone, a region between hemes 1 and 2 has more flexibility than the other regions. The results of this work strongly suggest that the cooperative reduction of hemes 1 and 2 is based on the conformational changes of the C-13 propionate of heme 1 and the aromatic ring of Tyr43, and the interaction between His34 and His 35 through covalent and coordination bonds.

PubMed: 12054869
DOI: 10.1016/S0022-2836(02)00367-4

Experimental method

SOLUTION NMR