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PDBsum entry 1ou0

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protein Protein-protein interface(s) links
Isomerase PDB id
1ou0
Jmol
Contents
Protein chains
190 a.a. *
Waters ×627
* Residue conservation analysis
PDB id:
1ou0
Name: Isomerase
Title: Precorrin-8x methylmutase related protein
Structure: Precorrin-8x methylmutase related protein. Chain: a, b, c, d. Engineered: yes
Source: Thermoplasma acidophilum dsm 1728. Organism_taxid: 273075. Strain: dsm1728. Gene: ta0654. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Tetramer (from PQS)
Resolution:
2.10Å     R-factor:   0.202     R-free:   0.235
Authors: M.E.Cuff,A.Joachimiak,S.Korolev,A.Savchenko,A.Edwards, Midwest Center For Structural Genomics (Mcsg)
Key ref:
M.E.Cuff et al. (2005). Crystal structure of a predicted precorrin-8x methylmutase from Thermoplasma acidophilum. Proteins, 58, 751-754. PubMed id: 15609338 DOI: 10.1002/prot.20022
Date:
24-Mar-03     Release date:   07-Oct-03    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9HKE7  (Q9HKE7_THEAC) -  Precorrin-8X methylmutase related protein
Seq:
Struc:
207 a.a.
190 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cobalamin biosynthetic process   1 term 
  Biochemical function     precorrin-8X methylmutase activity     1 term  

 

 
DOI no: 10.1002/prot.20022 Proteins 58:751-754 (2005)
PubMed id: 15609338  
 
 
Crystal structure of a predicted precorrin-8x methylmutase from Thermoplasma acidophilum.
M.E.Cuff, D.J.Miller, S.Korolev, X.Xu, W.F.Anderson, A.Edwards, A.Joachimiak, A.Savchenko.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Ribbon drawing of the T. acidophilum precorrin-8x methylmutase. Secondary structure elements are colored from N- to C-terminus, blue to red.
Figure 2.
Figure 2. C superposition of the T. acidophilum structure and P. denitrificans precorrin-8x methylmutase with product bound. For simplicity, only the A/D dimer is shown, and C positions numbered for polypeptide A (colored blue). In the view shown, the 2-fold axis is horizontal. The Pa2905 dimer (the biologically relevant oligomerization state) is colored tan. The active site is formed by the dimer interface, as evidenced by the bound precorrin product hydrogenobyrinic acid (HBA) colored yellow, with nitrogens colored blue, and oxygens red. The Pa2905 dimer was generated by crystallographic 2-fold symmetry. For clarity, only HBA observed in the asymmetric unit is shown.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 58, 751-754) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16154351 B.Zheng, C.J.Gerdts, and R.F.Ismagilov (2005).
Using nanoliter plugs in microfluidics to facilitate and understand protein crystallization.
  Curr Opin Struct Biol, 15, 548-555.  
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