4UOV

The structure of a tetrameric alpha-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides, which contribute to its thermostability.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.173 

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Literature

The Structure of a Tetrameric [Alpha]-Carbonic Anhydrase from Thermovibrio Ammonificans Reveals a Core Formed Around Intermolecular Disulfides that Contribute to its Thermostability

James, P.Isupov, M.N.Sayer, C.Saneei, V.Berg, S.Lioliou, M.Kotlar, H.Littlechild, J.

(2014) Acta Crystallogr D Biol Crystallogr 70: 2607

  • DOI: https://doi.org/10.1107/S1399004714016526
  • Primary Citation of Related Structures:  
    4C3T, 4COQ, 4UOV

  • PubMed Abstract: 

    Carbonic anhydrase enzymes catalyse the reversible hydration of carbon dioxide to bicarbonate. A thermophilic Thermovibrio ammonificans α-carbonic anhydrase (TaCA) has been expressed in Escherichia coli and structurally and biochemically characterized. The crystal structure of TaCA has been determined in its native form and in two complexes with bound inhibitors. The tetrameric enzyme is stabilized by a unique core in the centre of the molecule formed by two intersubunit disulfides and a single lysine residue from each monomer that is involved in intersubunit ionic interactions. The structure of this core protects the intersubunit disulfides from reduction, whereas the conserved intrasubunit disulfides are not formed in the reducing environment of the E. coli host cytosol. When oxidized to mimic the environment of the periplasmic space, TaCA has increased thermostability, retaining 90% activity after incubation at 70°C for 1 h, making it a good candidate for industrial carbon-dioxide capture. The reduction of all TaCA cysteines resulted in dissociation of the tetrameric molecule into monomers with lower activity and reduced thermostability. Unlike other characterized α-carbonic anhydrases, TaCA does not display esterase activity towards p-nitrophenyl acetate, which appears to result from the increased rigidity of its protein scaffold.


  • Organizational Affiliation

    Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CARBONATE DEHYDRATASE
A, B, C, D, E
A, B, C, D, E, F
247Thermovibrio ammonificansMutation(s): 0 
EC: 4.2.1.1
UniProt
Find proteins for E8T502 (Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1))
Explore E8T502 
Go to UniProtKB:  E8T502
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupE8T502
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 10 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PE3
Query on PE3

Download Ideal Coordinates CCD File 
DB [auth F],
I [auth A],
S [auth B]
3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL
C28 H58 O15
ILLKMACMBHTSHP-UHFFFAOYSA-N
B3P
Query on B3P

Download Ideal Coordinates CCD File 
EA [auth C],
EB [auth F],
J [auth A],
NA [auth D],
UA [auth E]
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
C11 H26 N2 O6
HHKZCCWKTZRCCL-UHFFFAOYSA-N
AZM
Query on AZM

Download Ideal Coordinates CCD File 
CB [auth F]
DA [auth C]
H [auth A]
MA [auth D]
R [auth B]
CB [auth F],
DA [auth C],
H [auth A],
MA [auth D],
R [auth B],
TA [auth E]
5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
C4 H6 N4 O3 S2
BZKPWHYZMXOIDC-UHFFFAOYSA-N
PG5
Query on PG5

Download Ideal Coordinates CCD File 
AA [auth B]1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE
C8 H18 O4
YFNKIDBQEZZDLK-UHFFFAOYSA-N
PGE
Query on PGE

Download Ideal Coordinates CCD File 
IA [auth C],
JB [auth F],
QA [auth D],
W [auth B],
XA [auth E]
TRIETHYLENE GLYCOL
C6 H14 O4
ZIBGPFATKBEMQZ-UHFFFAOYSA-N
TLA
Query on TLA

Download Ideal Coordinates CCD File 
HB [auth F],
O [auth A],
X [auth B]
L(+)-TARTARIC ACID
C4 H6 O6
FEWJPZIEWOKRBE-JCYAYHJZSA-N
PEG
Query on PEG

Download Ideal Coordinates CCD File 
AB [auth E]
BA [auth B]
KA [auth C]
KB [auth F]
LB [auth F]
AB [auth E],
BA [auth B],
KA [auth C],
KB [auth F],
LB [auth F],
N [auth A],
Z [auth B],
ZA [auth E]
DI(HYDROXYETHYL)ETHER
C4 H10 O3
MTHSVFCYNBDYFN-UHFFFAOYSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
FA [auth C]
FB [auth F]
K [auth A]
OA [auth D]
T [auth B]
FA [auth C],
FB [auth F],
K [auth A],
OA [auth D],
T [auth B],
VA [auth E]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
ZN
Query on ZN

Download Ideal Coordinates CCD File 
BB [auth F]
CA [auth C]
G [auth A]
LA [auth D]
Q [auth B]
BB [auth F],
CA [auth C],
G [auth A],
LA [auth D],
Q [auth B],
SA [auth E]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
GA [auth C]
GB [auth F]
HA [auth C]
IB [auth F]
JA [auth C]
GA [auth C],
GB [auth F],
HA [auth C],
IB [auth F],
JA [auth C],
L [auth A],
M [auth A],
P [auth A],
PA [auth D],
RA [auth D],
U [auth B],
V [auth B],
WA [auth E],
Y [auth B],
YA [auth E]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.173 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 163.75α = 90
b = 283.02β = 90
c = 52.17γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
xia2data reduction
Aimlessdata scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-10-15
    Type: Initial release
  • Version 1.1: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description