4G7A

The crystal structure of an alpha Carbonic Anhydrase from the extremophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.168 

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This is version 1.1 of the entry. See complete history


Literature

X-ray structure of the first `extremo-{alpha}-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1.

Di Fiore, A.Capasso, C.De Luca, V.Monti, S.M.Carginale, V.Supuran, C.T.Scozzafava, A.Pedone, C.Rossi, M.De Simone, G.

(2013) Acta Crystallogr D Biol Crystallogr 69: 1150-1159

  • DOI: https://doi.org/10.1107/S0907444913007208
  • Primary Citation of Related Structures:  
    4G7A

  • PubMed Abstract: 

    SspCA, a novel `extremo-α-carbonic anhydrase' isolated from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1, is an efficient catalyst for the hydration of CO2 and presents exceptional thermostability. Indeed, SspCA retains a high catalytic activity even after being heated to 343-373 K for several hours. Here, the crystallographic structure of this α-carbonic anhydrase (α-CA) is reported and the factors responsible for its function at high temperature are elucidated. In particular, the study suggests that increased structural compactness, together with an increased number of charged residues on the protein surface and a greater number of ionic networks, seem to be the key factors involved in the higher thermostability of this enzyme with respect to its mesophilic homologues. These findings are of extreme importance, since they provide a structural basis for the understanding of the mechanisms responsible for thermal stability in the α-CA family for the first time. The data obtained offer a tool that can be exploited to engineer α-CAs in order to obtain enzymes with enhanced thermostability for use in the harsh conditions of the CO2 capture and sequestration processes.


  • Organizational Affiliation

    Istituto di Biostrutture e Bioimmagini - CNR, Via Mezzocannone 16, 80134 Napoli, Italy.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbonate dehydratase
A, B
248Sulfurihydrogenibium sp. YO3AOP1Mutation(s): 0 
Gene Names: SYO3AOP1_0578
EC: 4.2.1.1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
AZM BindingDB:  4G7A Ki: 4.5 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.168 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.5α = 90
b = 68.36β = 106.03
c = 74.69γ = 90
Software Package:
Software NamePurpose
CrystalCleardata collection
AMoREphasing
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-05-29
    Type: Initial release
  • Version 1.1: 2013-06-19
    Changes: Database references