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Transferase PDB id
1shk
Jmol
Contents
Protein chains
158 a.a. *
Metals
_MG ×3
Waters ×473
* Residue conservation analysis
PDB id:
1shk
Name: Transferase
Title: The three-dimensional structure of shikimate kinase from erw chrysanthemi
Structure: Shikimate kinase. Chain: a, b. Engineered: yes
Source: Erwinia chrysanthemi. Organism_taxid: 556. Strain: ncppb 1066. Cellular_location: cytoplasm. Gene: arol. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: (de3) plyss.
Biol. unit: Monomer (from PDB file)
Resolution:
1.90Å     R-factor:   0.174     R-free:   0.222
Authors: T.Krell,J.R.Coggins,A.J.Lapthorn
Key ref:
T.Krell et al. (1997). Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi. Acta Crystallogr D Biol Crystallogr, 53, 612-614. PubMed id: 15299895 DOI: 10.1107/S0907444997004319
Date:
27-Oct-97     Release date:   18-Nov-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P10880  (AROL_ERWCH) -  Shikimate kinase 2
Seq:
Struc: 		173 a.a.
158 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.71  - Shikimate kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Shikimate and Chorismate Biosynthesis
      Reaction: ATP + shikimate = ADP + shikimate 3-phosphate
ATP
 + shikimate
 = ADP
 + shikimate 3-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     phosphorylation   3 terms 
  Biochemical function     nucleotide binding     6 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444997004319 Acta Crystallogr D Biol Crystallogr 53:612-614 (1997)
PubMed id: 15299895  
 
 
Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi.
T.Krell, J.E.Coyle, M.J.Horsburgh, J.R.Coggins, A.J.Lapthorn.
 
  ABSTRACT  
 
Shikimate kinase from Erwinia chrysanthemi, overexpressed in Escherichia coli has been crystallized by the vapour-diffusion method using sodium chloride as a precipitant. Mass spectrometry was used to confirm the purity of the shikimate kinase and dynamic light scattering was used to assess conditions for the monodispersity of the enzyme. The crystals are tetragonal, space group P4(1)2(1)2 or enantiomorph with cell dimensions a = b = 108.5 and c = 92.8 A (at 100 K). Native crystals diffract to better than 2.6 A on a synchrotron X-ray source. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 3.6 A(3) Da(-1).
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. A pseudo precession plot of the hOl zone extending to 3.0,~ calculated using the PATTERN program (G. Lu, unpublished work) showing the systematic absences.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1997, 53, 612-614) copyright 1997.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
11985590 E.Cerasoli, S.M.Kelly, J.R.Coggins, D.J.Boam, D.T.Clarke, and N.C.Price (2002).
The refolding of type II shikimate kinase from Erwinia chrysanthemi after denaturation in urea.
  Eur J Biochem, 269, 2124-2132.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.