6EKI

Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.56 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.164 
  • R-Value Observed: 0.168 

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This is version 1.2 of the entry. See complete history


Literature

Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney.

Fredslund, F.Borchert, M.S.Poulsen, J.N.Mortensen, S.B.Perner, M.Streit, W.R.Lo Leggio, L.

(2018) Enzyme Microb Technol 114: 48-54

  • DOI: https://doi.org/10.1016/j.enzmictec.2018.03.009
  • Primary Citation of Related Structures:  
    6EKI

  • PubMed Abstract: 

    Carbonic anhydrases (CAs) are extremely fast enzymes, which have attracted much interest in the past due to their medical relevance and their biotechnological potential. An α-type CA gene was isolated from DNA derived from an active hydrothermal vent chimney, in an effort to identify novel CAs with suitable properties for CO 2 capture. The gene product was recombinantly produced and characterized, revealing remarkable thermostability, also in the presence of high ionic strength alkaline conditions, which are used in some CO 2 capture applications. The T m was above 90 °C under all tested conditions. The enzyme was crystallized and the structure determined by molecular replacement, revealing a typical bacterial α-type CA non-covalent dimer, but not the disulphide mediated tetramer observed for the hyperthermophilic homologue used for molecular replacement, from Thermovibrio ammonificans. Structural comparison suggests that an increased secondary structure content, increased content of charges on the surface and ionic interactions compared to mesophilic enzymes, may be main structural sources of thermostability, as previously suggested for the homologue from Sulfurihydrogenibium yellowstonense.


  • Organizational Affiliation

    Department of Chemistry, University of Copenhagen, Universitetsparken 5, Copenhagen, DK-2100, Denmark.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbonic anhydrase
A, B, C, D, E
A, B, C, D, E, F
226Persephonella marinaMutation(s): 0 
EC: 4.2.1.1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.56 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.164 
  • R-Value Observed: 0.168 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.317α = 88.38
b = 71.276β = 82.84
c = 103.344γ = 84.22
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-04-11
    Type: Initial release
  • Version 1.1: 2018-05-02
    Changes: Data collection, Database references
  • Version 1.2: 2024-01-17
    Changes: Data collection, Database references, Refinement description