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PDBsum entry 2xia

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Isomerase(intramolecular oxidoreductse) PDB id
2xia
Jmol
Contents
Protein chain
382 a.a.*
* C-alpha coords only
Superseded by: 7xia
PDB id:
2xia
Name: Isomerase(intramolecular oxidoreductse)
Structure: D- Xylose isomerase
Source: (Streptomyces rubiginosus)
Authors: H.L.Carrell
Key ref: K.Henrick et al. (1987). Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter. Protein Eng, 1, 467-469. PubMed id: 3508294
Date:
26-May-88     Release date:   09-Oct-88    
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 382 a.a.
Key:    Secondary structure

 

 
    Key reference    
 
 
Protein Eng 1:467-469 (1987)
PubMed id: 3508294  
 
 
Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter.
K.Henrick, D.M.Blow, H.L.Carrell, J.P.Glusker.
 
  ABSTRACT  
 
The C alpha backbones of the glucose isomerase molecules of Streptomyces rubiginosus and Arthrobacter have been determined by X-ray crystallography and compared. Each molecule is a tetramer of eight-stranded alpha/beta barrels, and the mode of association of the tetramers is identical in each case. The Arthrobacter electron density shows four additional amino acids at the carboxyl terminus. There is also an insertion of six amino acids at position 277, and two individual insertions at about positions 348 and 357 (numbering according to the Streptomyces structure). There is a close structural homology throughout the whole molecule, which is most accurate up to position 325. The r.m.s. displacement for 315 homologous C alpha positions up to this position is 0.92 A.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
10666592 X.Zhu, M.Teng, L.Niu, C.Xu, and Y.Wang (2000).
Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution.
  Acta Crystallogr D Biol Crystallogr, 56, 129-136.
PDB codes: 1clk 1qt1
8451241 N.Vtyurin (1993).
The role of local tight packing of hydrophobic groups in beta-structure.
  Proteins, 15, 62-70.  
  1657868 H.C.Wong, Y.Ting, H.C.Lin, F.Reichert, K.Myambo, K.W.Watt, P.L.Toy, and R.J.Drummond (1991).
Genetic organization and regulation of the xylose degradation genes in Streptomyces rubiginosus.
  J Bacteriol, 173, 6849-6858.  
2006134 M.Whitlow, A.J.Howard, B.C.Finzel, T.L.Poulos, E.Winborne, and G.L.Gilliland (1991).
A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose.
  Proteins, 9, 153-173.
PDB codes: 1xis 2xis 3xis 4xis
1367634 W.J.Quax, N.T.Mrabet, R.G.Luiten, P.W.Schuurhuizen, P.Stanssens, and I.Lasters (1991).
Enhancing the thermostability of glucose isomerase by protein engineering.
  Biotechnology (N Y), 9, 738-742.  
2405386 C.A.Batt, A.C.Jamieson, and M.A.Vandeyar (1990).
Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase.
  Proc Natl Acad Sci U S A, 87, 618-622.  
2304904 C.A.Collyer, and D.M.Blow (1990).
Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase.
  Proc Natl Acad Sci U S A, 87, 1362-1366.
PDB codes: 1did 1die
2362946 I.Lasters, S.J.Wodak, and F.Pio (1990).
The design of idealized alpha/beta-barrels: analysis of beta-sheet closure requirements.
  Proteins, 7, 249-256.  
2734296 H.L.Carrell, J.P.Glusker, V.Burger, F.Manfre, D.Tritsch, and J.F.Biellmann (1989).
X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator.
  Proc Natl Acad Sci U S A, 86, 4440-4444.
PDB codes: 7xia 8xia 9xia
3237716 F.Rey, J.Jenkins, J.Janin, I.Lasters, P.Alard, M.Claessens, G.Matthyssens, and S.Wodak (1988).
Structural analysis of the 2.8 A model of Xylose isomerase from Actinoplanes missouriensis.
  Proteins, 4, 165-172.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.