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PDBsum entry 1i60

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protein links
Structural genomics, unknown function PDB id
1i60
Jmol
Contents
Protein chain
278 a.a. *
Waters ×182
* Residue conservation analysis
PDB id:
1i60
Name: Structural genomics, unknown function
Title: Structural genomics, ioli protein
Structure: Ioli protein. Chain: a. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Gene: ioli or b65b. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.60Å     R-factor:   0.214     R-free:   0.228
Authors: R.Zhang,I.Dementieva,F.Collart,E.Quaite-Randall, A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)
Key ref:
R.G.Zhang et al. (2002). Crystal structure of Bacillus subtilis ioli shows endonuclase IV fold with altered Zn binding. Proteins, 48, 423-426. PubMed id: 12112707 DOI: 10.1002/prot.10159
Date:
01-Mar-01     Release date:   13-Mar-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P42419  (IOLI_BACSU) -  Inosose isomerase
Seq:
Struc:
278 a.a.
278 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.3.99.11  - 2-keto-myo-inositol isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2,4,6/3,5-pentahydroxycyclohexanone = 2D-2,3,5/4,6- pentahydroxycyclohexanone
2,4,6/3,5-pentahydroxycyclohexanone
= 2D-2,3,5/4,6- pentahydroxycyclohexanone
      Cofactor: Divalent cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     isomerase activity     2 terms  

 

 
    Key reference    
 
 
DOI no: 10.1002/prot.10159 Proteins 48:423-426 (2002)
PubMed id: 12112707  
 
 
Crystal structure of Bacillus subtilis ioli shows endonuclase IV fold with altered Zn binding.
R.G.Zhang, I.Dementieva, N.Duke, F.Collart, E.Quaite-Randall, R.Alkire, L.Dieckman, N.Maltsev, O.Korolev, A.Joachimiak.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Structure of IolI protein and its metal-binding site. a: Ribbon diagram showing the spatial arrangement of -helices and -sheets comprising beta barrel conformation adopted by IolI protein. Side-chains of conserved residues are shown, including those coordinating Zn ion (green). View is approximately perpendicular to the axis of the barrel. b: 2Fo-Fc map of IolI protein in the presence of 2 mM ZnCl[2]. c: 2Fo-Fc map of IolI protein in the presence of 2 mM MnCl[2]. A water molecule (H[2]O92) is residing in roughly the same location as the zinc atom of Figure 1(b).
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2002, 48, 423-426) copyright 2002.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18955706 B.F.Pfleger, Y.Kim, T.D.Nusca, N.Maltseva, J.Y.Lee, C.M.Rath, J.B.Scaglione, B.K.Janes, E.C.Anderson, N.H.Bergman, P.C.Hanna, A.Joachimiak, and D.H.Sherman (2008).
Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis.
  Proc Natl Acad Sci U S A, 105, 17133-17138.
PDB code: 3dx5
18515839 M.Gao, and J.Skolnick (2008).
DBD-Hunter: a knowledge-based method for the prediction of DNA-protein interactions.
  Nucleic Acids Res, 36, 3978-3992.  
18849419 R.Shi, M.Pineda, E.Ajamian, Q.Cui, A.Matte, and M.Cygler (2008).
Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold.
  J Bacteriol, 190, 8137-8144.
PDB codes: 3cqh 3cqi 3cqj 3cqk
16461681 K.Yoshida, M.Yamaguchi, T.Morinaga, M.Ikeuchi, M.Kinehara, and H.Ashida (2006).
Genetic modification of Bacillus subtilis for production of D-chiro-inositol, an investigational drug candidate for treatment of type 2 diabetes and polycystic ovary syndrome.
  Appl Environ Microbiol, 72, 1310-1315.  
15558595 F.J.Stevens (2005).
Efficient recognition of protein fold at low sequence identity by conservative application of Psi-BLAST: validation.
  J Mol Recognit, 18, 139-149.  
15263850 Y.Kim, I.Dementieva, M.Zhou, R.Wu, L.Lezondra, P.Quartey, G.Joachimiak, O.Korolev, H.Li, and A.Joachimiak (2004).
Automation of protein purification for structural genomics.
  J Struct Funct Genomics, 5, 111-118.  
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 code is shown on the right.