1C7M

SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS DENITRIFICANS CYTOCHROME C552 IN THE REDUCED STATE

Summary for 1C7M

• Entry DOI: 10.2210/pdb1c7m/pdb
• Descriptor: PROTEIN (CYTOCHROME C552), HEME C (2 entities in total)
• Functional Keywords: electron transport, cytochrome c552, heme, redox states, isotope enrichment {15n}, nmr spectroscopy, solution structure
• Biological source: Paracoccus denitrificans
• Cellular location: Cell membrane; Single-pass membrane protein: P54820
• Total number of polymer chains: 1
• Total formula weight: 11172.48

Authors

Pristovsek, P.,Luecke, C.,Reincke, B.,Ludwig, B.,Rueterjans, H. (deposition date: 2000-03-03, release date: 2000-07-19, Last modification date: 2024-10-30)

Primary citation

Pristovsek, P.,Lucke, C.,Reincke, B.,Ludwig, B.,Ruterjans, H.
Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state.
Eur.J.Biochem., 267:4205-4212, 2000

PubMed Abstract: In order to determine the solution structure of Paracoccus denitrificans cytochrome c552 by NMR, we cloned and isotopically labeled a 10.5-kDa soluble fragment (100 residues) containing the functional domain of the 18.2-kDa membrane-bound protein. Using uniformly 15N-enriched samples of cytochrome c552 in the reduced state, a variety of two-dimensional and three-dimensional heteronuclear double-resonance NMR experiments was employed to achieve complete 1H and 15N assignments. A total of 1893 distance restraints was derived from homonuclear 2D-NOESY and heteronuclear 3D-NOESY spectra; 1486 meaningful restraints were used in the structure calculations. After restrained energy minimization a family of 20 structures was obtained with rmsd values of 0.56 +/- 0. 10 A and 1.09 +/- 0.09 A for the backbone and heavy atoms, respectively. The overall topology is similar to that seen in previously reported models of this class of proteins. The global fold consists of two long helices at the N-terminus and C-terminus and three shorter helices surrounding the heme moiety; the helices are connected by well-defined loops. Comparison with the X-ray structure shows some minor differences in the positions of the Trp57 and Phe65 side-chain rings as well as the heme propionate groups.

PubMed: 10866825
DOI: 10.1046/j.1432-1327.2000.01456.x

Experimental method

SOLUTION NMR