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PDBsum entry 1itz

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1itz
Jmol
Contents
Protein chains
666 a.a. *
Ligands
TPP ×3
Metals
_MG ×3
Waters ×440
* Residue conservation analysis
PDB id:
1itz
Name: Transferase
Title: Maize transketolase in complex with tpp
Structure: Transketolase. Chain: a, b, c. Engineered: yes
Source: Zea mays. Organism_taxid: 4577. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.30Å     R-factor:   0.166     R-free:   0.200
Authors: S.Gerhardt,S.Echt,G.Bader,J.Freigang,M.Busch,A.Bacher, R.Huber,M.Fischer
Key ref: S.Gerhardt et al. (2003). Structure and properties of an engineered transketolase from maize. Plant Physiol, 132, 1941-1949. PubMed id: 12913150
Date:
15-Feb-02     Release date:   15-Feb-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7SIC9  (TKTC_MAIZE) -  Transketolase, chloroplastic
Seq:
Struc:
 
Seq:
Struc:
675 a.a.
666 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.2.1.1  - Transketolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Sedoheptulose 7-phosphate
+ D-glyceraldehyde 3-phosphate
= D-ribose 5-phosphate
+ D-xylulose 5-phosphate
      Cofactor: Thiamine diphosphate
Thiamine diphosphate
Bound ligand (Het Group name = TPP) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   6 terms 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    reference    
 
 
Plant Physiol 132:1941-1949 (2003)
PubMed id: 12913150  
 
 
Structure and properties of an engineered transketolase from maize.
S.Gerhardt, S.Echt, M.Busch, J.Freigang, G.Auerbach, G.Bader, W.F.Martin, A.Bacher, R.Huber, M.Fischer.
 
  ABSTRACT  
 
The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19052774 B.C.Willige, M.Kutzer, F.Tebartz, and D.Bartels (2009).
Subcellular localization and enzymatic properties of differentially expressed transketolase genes isolated from the desiccation tolerant resurrection plant Craterostigma plantagineum.
  Planta, 229, 659-666.  
17850260 F.Domain, X.R.Bina, and S.B.Levy (2007).
Transketolase A, an enzyme in central metabolism, derepresses the marRAB multiple antibiotic resistance operon of Escherichia coli by interaction with MarR.
  Mol Microbiol, 66, 383-394.  
16817154 N.Izawa, M.Kishimoto, M.Konishi, T.Omasa, S.Shioya, and H.Ohtake (2006).
Recognition of culture state using two-dimensional gel electrophoresis with an artificial neural network.
  Proteomics, 6, 3730-3738.  
16125202 O.A.Esakova, L.E.Meshalkina, and G.A.Kochetov (2005).
Effects of transketolase cofactors on its conformation and stability.
  Life Sci, 78, 8.  
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.