6ELQ

Carbon Monoxide Dehydrogenase IV from Carboxydothermus hydrogenoformans


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.236 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2.

Domnik, L.Merrouch, M.Goetzl, S.Jeoung, J.H.Leger, C.Dementin, S.Fourmond, V.Dobbek, H.

(2017) Angew Chem Int Ed Engl 56: 15466-15469

  • DOI: https://doi.org/10.1002/anie.201709261
  • Primary Citation of Related Structures:  
    6ELQ

  • PubMed Abstract: 

    CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO 2 . Genomic analysis indicated that the metabolic functions of CODHs vary. The genome of Carboxydothermus hydrogenoformans encodes five CODHs (CODH-I-V), of which CODH-IV is found in a gene cluster near a peroxide-reducing enzyme. Our kinetic and crystallographic experiments reveal that CODH-IV differs from other CODHs in several characteristic properties: it has a very high affinity for CO, oxidizes CO at diffusion-limited rate over a wide range of temperatures, and is more tolerant to oxygen than CODH-II. Thus, our observations support the idea that CODH-IV is a CO scavenger in defence against oxidative stress and highlight that CODHs are more diverse in terms of reactivity than expected.


  • Organizational Affiliation

    Institut für Biologie, Strukturbiologie/Biochemie, Humboldt-Universität zu Berlin, Unter den Linden 6, 10099, Berlin, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbon Monoxide DehydrogenaseA [auth X],
B [auth A],
C [auth B]
633Carboxydothermus hydrogenoformansMutation(s): 0 
Gene Names: cooSIV
EC: 1.2.7.4
UniProt
Find proteins for Q3AE44 (Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901))
Explore Q3AE44 
Go to UniProtKB:  Q3AE44
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ3AE44
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.236 
  • Space Group: P 3 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 209.15α = 90
b = 209.15β = 90
c = 93.41γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-03
    Type: Initial release
  • Version 1.1: 2019-10-16
    Changes: Data collection