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1HRO

MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS

Summary for 1HRO
Entry DOI10.2210/pdb1hro/pdb
DescriptorCYTOCHROME C2, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordselectron transport, photosynthesis, heme
Biological sourceRhodopila globiformis
Total number of polymer chains2
Total formula weight24291.29
Authors
Benning, M.M.,Meyer, T.E.,Holden, H.M. (deposition date: 1996-07-10, release date: 1997-01-11, Last modification date: 2024-06-05)
Primary citationBenning, M.M.,Meyer, T.E.,Holden, H.M.
Molecular structure of a high potential cytochrome c2 isolated from Rhodopila globiformis.
Arch.Biochem.Biophys., 333:338-348, 1996
Cited by
PubMed Abstract: Unlike their mitochondrial counterparts, the c-type cytochromes typically isolated from photosynthetic nonsulfur purple bacteria display a wide range of oxidation-reduction potentials. Here we describe the X-ray crystallographic analysis of the cytochrome c2 isolated from Rhodopila globiformis. This particular c-type cytochrome was selected for study because of its anomalously high redox potential of +450 mV. Crystals employed in the investigation belonged to the space group I4(1) with unit cell dimensions of a = b = 79.2 A, c = 75.2 A, and two molecules in the asymmetric unit. The structure was solved by the techniques of multiple isomorphous replacement with two heavy-atom derivatives and electron density modification procedures. Least-squares refinement of the model reduced the R-factor to 18.7% for all measured X-ray data from 30.0 to 2.2 A. The overall structural motif of the protein is composed of five alpha-helices, one type I turn, and six type II turns. As in other cytochromes c, there are two conserved water molecules located in the heme-binding pocket. Overall, the three-dimensional structure of the R. globiformis molecule is more similar to the eukaryotic c-type cytochromes than to other bacterial proteins.
PubMed: 8809072
DOI: 10.1006/abbi.1996.0400
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

226707

數據於2024-10-30公開中

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