High resolution crystal structure of ferricytochrome c' from Rhodobacter sphaeroides

Laura M.-Ramirez, Herbert L. Axelrod, Steven R. Herron, Bernhard Rupp, James Paul Allen, Katherine A. Kantardjieff

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14 Citations (Scopus)

Abstract

Cytochrome c' isolated from Rhodobacter sphaeroides strain R26 (RSCP) crystallizes as a dimer of two identical 14-kDa subunits, in trigonal space group P31, with cell parameters a, b = 48.10 Å, c = 115.80 Å. The crystal structure of RSCP has been solved by molecular replacement using cytochrome c' from Rhodobacter capsulatus (PDB ID: 1CPQ) as a search model. To ensure effective phase bias removal, the RSCP model was iteratively built into maps generated by a modified wARP procedure, Shake&wARP. The 1.8 Å model (PDB ID: 1GQA) has been refined to an R = 0.204 and freeR = 0.254. Each subunit consists of four antiparallel α-helices, with the pentacoordinate heme covalently bound to a C-X-Y-C-H motif near the C-terminus. F14, located on helix A, blocks direct access to what would be the sixth "distal" ligand binding site of the heme. The dimer subunits form a flattened "X" shape, intermediate between the Type 1 and Type 2 cytochromes c'. The presence of the aromatic F14 and a deep channel between helices B and C places RSCP into Group 1 cytochromes c'. Clear electron density has revealed that the amino acid sequences for the cytochrome c' from strains R26 and 2.4.1 are identical.

Original languageEnglish
Pages (from-to)413-424
Number of pages12
JournalJournal of Chemical Crystallography
Volume33
Issue number5-6
DOIs
Publication statusPublished - Jun 2003

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Keywords

  • Cytochrome c'
  • Four helix bundle
  • Heme protein
  • Rhodobacter sphaeroides

ASJC Scopus subject areas

  • Spectroscopy
  • Condensed Matter Physics
  • Structural Biology

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