2VAR

Crystal structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase complexed with 2-keto-3-deoxygluconate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.181 
  • R-Value Observed: 0.183 

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Literature

The Structure of Sulfolobus Solfataricus 2-Keto-3-Deoxygluconate Kinase.

Potter, J.A.Kerou, M.Lamble, H.J.Bull, S.D.Hough, D.W.Danson, M.J.Taylor, G.L.

(2008) Acta Crystallogr D Biol Crystallogr 64: 1283

  • DOI: https://doi.org/10.1107/S0907444908036111
  • Primary Citation of Related Structures:  
    2V78, 2VAR

  • PubMed Abstract: 

    The hyperthermophilic archaeon Sulfolobus solfataricus grows optimally above 353 K and utilizes an unusual promiscuous nonphosphorylative Entner-Doudoroff pathway to metabolize both glucose and galactose. It has been proposed that a part-phosphorylative Entner-Doudoroff pathway occurs in parallel in S. solfataricus, in which the 2-keto-3-deoxygluconate kinase (KDGK) is promiscuous for both glucose and galactose metabolism. Recombinant S. solfataricus KDGK protein was expressed in Escherichia coli, purified and crystallized in 0.1 M sodium acetate pH 4.1 and 1.4 M NaCl. The crystal structure of apo S. solfataricus KDGK was solved by molecular replacement to a resolution of 2.0 A and a ternary complex with 2-keto-3-deoxygluconate (KDGlu) and an ATP analogue was resolved at 2.1 A. The complex suggests that the structural basis for the enzyme's ability to phosphorylate KDGlu and 2-keto-3-deoxygalactonate (KDGal) is derived from a subtle repositioning of residues that are conserved in homologous nonpromiscuous kinases.


  • Organizational Affiliation

    Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, Scotland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FRUCTOKINASE
A, B, C
313Saccharolobus solfataricusMutation(s): 0 
EC: 2.7.1.4 (PDB Primary Data), 2.7.1.178 (UniProt)
UniProt
Find proteins for Q97U29 (Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2))
Explore Q97U29 
Go to UniProtKB:  Q97U29
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ97U29
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ANP
Query on ANP

Download Ideal Coordinates CCD File 
F [auth A],
J [auth B],
N [auth C]
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
C10 H17 N6 O12 P3
PVKSNHVPLWYQGJ-KQYNXXCUSA-N
AMP
Query on AMP

Download Ideal Coordinates CCD File 
G [auth A],
K [auth B],
O [auth C]
ADENOSINE MONOPHOSPHATE
C10 H14 N5 O7 P
UDMBCSSLTHHNCD-KQYNXXCUSA-N
KDG
Query on KDG

Download Ideal Coordinates CCD File 
D [auth A],
H [auth B],
L [auth C]
2-KETO-3-DEOXYGLUCONATE
C6 H10 O6
WPAMZTWLKIDIOP-WVZVXSGGSA-N
KDF
Query on KDF

Download Ideal Coordinates CCD File 
E [auth A],
I [auth B],
M [auth C]
3-deoxy-alpha-D-erythro-hex-2-ulofuranosonic acid
C6 H10 O6
RCUMQJPRQWRUNN-MRKVFDINSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.181 
  • R-Value Observed: 0.183 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 104.553α = 90
b = 104.553β = 90
c = 420.782γ = 120
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-02
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Derived calculations, Other
  • Version 2.1: 2024-05-08
    Changes: Data collection, Database references, Structure summary