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PDBsum entry 1bhw

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protein Protein-protein interface(s) links
Isomerase PDB id
1bhw
Jmol
Contents
Protein chains
392 a.a. *
* Residue conservation analysis
PDB id:
1bhw
Name: Isomerase
Title: Low temperature middle resolution structure of xylose isomerase from masc data
Structure: Xylose isomerase. Chain: a, b, c, d. Engineered: yes. Mutation: yes
Source: Actinoplanes missouriensis. Organism_taxid: 1866. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PDB file)
Resolution:
4.10Å     R-factor:   0.315     R-free:   0.321
Authors: M.Ramin,W.Shepard,R.Fourme,R.Kahn
Key ref:
M.Ramin et al. (1999). Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values. Acta Crystallogr D Biol Crystallogr, 55, 157-167. PubMed id: 10089406 DOI: 10.1107/S090744499800626X
Date:
10-Jun-98     Release date:   04-Nov-98    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P12851  (XYLA_ACTMI) -  Xylose isomerase
Seq:
Struc:
394 a.a.
392 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.5.3.1.5  - Xylose isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-xylopyranose = D-xylulose
D-xylopyranose
= D-xylulose
      Cofactor: Magnesium
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     carbohydrate metabolic process   3 terms 
  Biochemical function     isomerase activity     4 terms  

 

 
    Key reference    
 
 
DOI no: 10.1107/S090744499800626X Acta Crystallogr D Biol Crystallogr 55:157-167 (1999)
PubMed id: 10089406  
 
 
Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.
M.Ramin, W.Shepard, R.Fourme, R.Kahn.
 
  ABSTRACT  
 
A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d >/= 20 A), the agreement between experimental {GammaT(h)} and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental {GammaT(h)} and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.
 
  Selected figure(s)  
 
Figure 5.
Figure 5 Section z = 0 of the phased anomalous Fourier-difference map of P64k in 3.5 M (NH[4])[2]SeO[4] contoured at 3 above the mean density superimposed with an envelope model section of P64k at low temperature.
Figure 7.
Figure 7 Section z = 0.094 of the phased anomalous Fourier-difference map of HEWL in 0.5 M YbCl[3] contoured at 3 above the mean density superimposed with an envelope model section of HEWL at low temperature. The Yb atoms are located near the surface and/or in crevices.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 157-167) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference Google scholar

  PubMed id Reference
18156683 H.B.Stuhrmann (2008).
Small-angle scattering and its interplay with crystallography, contrast variation in SAXS and SANS.
  Acta Crystallogr A, 64, 181-191.  
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