3CP5

Cytochrome c from rhodothermus marinus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.24 Å
  • R-Value Free: 0.174 
  • R-Value Observed: 0.130 

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This is version 1.2 of the entry. See complete history


Literature

A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of rhodothermus marinus cytochrome c

Stelter, M.Melo, A.M.Pereira, M.M.Gomes, C.M.Hreggvidsson, G.O.Hjorleifsdottir, S.Saraiva, L.M.Teixeira, M.Archer, M.

(2008) Biochemistry 47: 11953-11963

  • DOI: https://doi.org/10.1021/bi800999g
  • Primary Citation of Related Structures:  
    3CP5

  • PubMed Abstract: 

    Monoheme cytochromes of the C-type are involved in a large number of electron transfer processes, which play an essential role in multiple pathways, such as respiratory chains, either aerobic or anaerobic, and the photosynthetic electron transport chains. This study reports the biochemical characterization and the crystallographic structure, at 1.23 A resolution, of a monoheme cytochrome c from the thermohalophilic bacterium Rhodothermus marinus. In addition to an alpha-helical core folded around the heme, common for this type of cytochrome, the X-ray structure reveals one unusual alpha-helix and a unique N-terminal extension, which wraps around the back of the molecule. Based on a thorough structural and amino acid sequence comparison, we propose R. marinus cytochrome c as the first characterized member of a new class of C-type cytochromes.


  • Organizational Affiliation

    Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome c124Rhodothermus marinusMutation(s): 0 
Gene Names: cytC
UniProt
Find proteins for B3FQS5 (Rhodothermus marinus)
Explore B3FQS5 
Go to UniProtKB:  B3FQS5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB3FQS5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.24 Å
  • R-Value Free: 0.174 
  • R-Value Observed: 0.130 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 39.592α = 90
b = 32.644β = 94.56
c = 42.064γ = 90
Software Package:
Software NamePurpose
SHELXmodel building
SHELXL-97refinement
MxCuBEdata collection
MOSFLMdata reduction
CCP4data scaling
SHELXphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-10-28
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-10-30
    Changes: Data collection, Database references, Derived calculations, Structure summary