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Structural genomics, unknown function PDB id
3iwt
Jmol
Contents
Protein chains
166 a.a. *
Ligands
PEG ×8
GOL ×2
Metals
_MG ×2
Waters ×582
* Residue conservation analysis
PDB id:
3iwt
Name: Structural genomics, unknown function
Title: Structure of hypothetical molybdenum cofactor biosynthesis p from sulfolobus tokodaii
Structure: 178aa long hypothetical molybdenum cofactor biosy protein b. Chain: a, b, c. Engineered: yes
Source: Sulfolobus tokodaii. Organism_taxid: 111955. Strain: 7, dsm 16993, jcm 10545, nbrc 100140. Gene: st2315. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.169     R-free:   0.187
Authors: S.V.Antonyuk,M.J.Ellis,R.W.Strange,S.S.Hasnain,Y.Bessho,S.Ku S.Yokoyama,Riken Structural Genomics/proteomics Initiative
Key ref: S.V.Antonyuk et al. (2009). Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from Sulfolobus tokodaii. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 1200-1203. PubMed id: 20054111 DOI: 10.1107/S1744309109043772
Date:
03-Sep-09     Release date:   29-Sep-09    
Supersedes: 2pjk
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q96Y52  (Q96Y52_SULTO) -  Molybdopterin biosynthesis protein MoaB
Seq:
Struc:
178 a.a.
166 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     Mo-molybdopterin cofactor biosynthetic process   1 term 

 

 
DOI no: 10.1107/S1744309109043772 Acta Crystallogr Sect F Struct Biol Cryst Commun 65:1200-1203 (2009)
PubMed id: 20054111  
 
 
Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from Sulfolobus tokodaii.
S.V.Antonyuk, R.W.Strange, M.J.Ellis, Y.Bessho, S.Kuramitsu, A.Shinkai, S.Yokoyama, S.S.Hasnain.
 
  ABSTRACT  
 
The structure of a probable Mo-cofactor biosynthesis protein B from Sulfolobus tokodaii, belonging to space group P6(4)22 with unit-cell parameters a = b = 136.68, c = 210.52 A, was solved by molecular replacement to a resolution of 1.9 A and refined to an R factor and R(free) of 16.8% and 18.5%, respectively. The asymmetric unit contains a trimer, while the biologically significant oligomer is predicted to be a hexamer by size-exclusion chromatography. The subunit structure and fold of ST2315 are similar to those of other enzymes that are known to be involved in the molybdopterin- and molybdenum cofactor-biosynthesis pathways.