spacer
spacer

PDBsum entry 1yiz

Go to PDB code: 
protein metals Protein-protein interface(s) links
Transferase PDB id
1yiz
Jmol
Contents
Protein chains
418 a.a. *
Metals
_BR ×5
Waters ×440
* Residue conservation analysis
PDB id:
1yiz
Name: Transferase
Title: Aedes aegypti kynurenine aminotrasferase
Structure: Kynurenine aminotransferase. Glutamine transaminase. Chain: a, b. Fragment: kynurenine aminotransferase (residues 49-477). Engineered: yes
Source: Aedes aegypti. Yellow fever mosquito. Organism_taxid: 7159. Gene: kat. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Biol. unit: Dimer (from PQS)
Resolution:
1.55Å     R-factor:   0.254     R-free:   0.279
Authors: Q.Han,Y.G.Gao,H.Robinson,H.Ding,S.Wilson,J.Li
Key ref:
Q.Han et al. (2005). Crystal structures of Aedes aegypti kynurenine aminotransferase. FEBS J, 272, 2198-2206. PubMed id: 15853804 DOI: 10.1111/j.1742-4658.2005.04643.x
Date:
13-Jan-05     Release date:   10-May-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q95VY4  (Q95VY4_AEDAE) -  Kynurenine aminotransferase
Seq:
Struc:
477 a.a.
418 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biosynthetic process   1 term 
  Biochemical function     catalytic activity     4 terms  

 

 
DOI no: 10.1111/j.1742-4658.2005.04643.x FEBS J 272:2198-2206 (2005)
PubMed id: 15853804  
 
 
Crystal structures of Aedes aegypti kynurenine aminotransferase.
Q.Han, Y.G.Gao, H.Robinson, H.Ding, S.Wilson, J.Li.
 
  ABSTRACT  
 
Aedes aegypti kynurenine aminotransferase (AeKAT) catalyzes the irreversible transamination of kynurenine to kynurenic acid, the natural antagonist of NMDA and 7-nicotinic acetycholine receptors. Here, we report the crystal structure of AeKAT in its PMP and PLP forms at 1.90 and 1.55 A, respectively. The structure was solved by a combination of single-wavelength anomalous dispersion and molecular replacement approaches. The initial search model in the molecular replacement method was built with the result of single-wavelength anomalous dispersion data from the Br-AeKAT crystal in combination with homology modeling. The solved structure shows that the enzyme is a homodimer, and that the two subunits are stabilized by a number of hydrogen bonds, salts bridges, and hydrophobic interactions. Each subunit is divided into an N-terminal arm and small and large domains. Based on its folding, the enzyme belongs to the prototypical fold type, aminotransferase subgroup I. The three-dimensional structure shows a strictly conserved 'PLP-phosphate binding cup' featuring PLP-dependent enzymes. The interaction between Cys284 (A) and Cys284 (B) is unique in AeKAT, which might explain the cysteine effect of AeKAT activity. Further mutation experiments of this residue are needed to eventually understand the mechanism of the enzyme modulation by cysteine.
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. Diagrams of 2F[o] – F[c] electron density maps for the active sites of the PMP and PLP forms. The map contoured at 2.0 sigma is calculated using data between 10.0 and 1.90 Å and 10.0 and 1.55 Å resolution for the PMP and PLP forms of AeKAT, respectively. (A) PLP form; (B) PMP form.
Figure 4.
Fig. 4. Schematic diagram showing active site interactions in AeKAT. Hydrogen bonds are shown by dotted lines. Phe135 and Val223 sandwich the pyridine ring of PLP. (A) PLP form; (B) PMP form.
 
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS J (2005, 272, 2198-2206) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19826765 Q.Han, T.Cai, D.A.Tagle, and J.Li (2010).
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.
  Cell Mol Life Sci, 67, 353-368.
PDB code: 3hlm
20482848 Q.Han, T.Cai, D.A.Tagle, and J.Li (2010).
Thermal stability, pH dependence and inhibition of four murine kynurenine aminotransferases.
  BMC Biochem, 11, 19.  
19381689 B.Battsetseg, D.Boldbaatar, B.Battur, X.Xuan, and K.Fujisaki (2009).
Cloning and molecular characterization of tick kynurenine aminotransferase (HlKAT) from Haemaphysalis longicornis (Acari: Ixodidae).
  Parasitol Res, 105, 669-679.  
19029248 Q.Han, H.Robinson, T.Cai, D.A.Tagle, and J.Li (2009).
Biochemical and structural properties of mouse kynurenine aminotransferase III.
  Mol Cell Biol, 29, 784-793.
PDB codes: 3e2f 3e2y 3e2z
19338303 Q.Han, H.Robinson, T.Cai, D.A.Tagle, and J.Li (2009).
Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K.
  J Med Chem, 52, 2786-2793.
PDB codes: 3fvs 3fvu 3fvx
18950711 F.Rossi, R.Schwarcz, and M.Rizzi (2008).
Curiosity to kill the KAT (kynurenine aminotransferase): structural insights into brain kynurenic acid synthesis.
  Curr Opin Struct Biol, 18, 748-755.  
18056996 F.Rossi, S.Garavaglia, V.Montalbano, M.A.Walsh, and M.Rizzi (2008).
Crystal Structure of Human Kynurenine Aminotransferase II, a Drug Target for the Treatment of Schizophrenia.
  J Biol Chem, 283, 3559-3566.
PDB code: 2vgz
18186649 Q.Han, Y.G.Gao, H.Robinson, and J.Li (2008).
Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase.
  Biochemistry, 47, 1622-1630.
PDB codes: 2r5c 2r5e
17070835 Q.Han, B.T.Beerntsen, and J.Li (2007).
The tryptophan oxidation pathway in mosquitoes with emphasis on xanthurenic acid biosynthesis.
  J Insect Physiol, 53, 254-263.  
16990263 Q.Han, H.Robinson, Y.G.Gao, N.Vogelaar, S.R.Wilson, M.Rizzi, and J.Li (2006).
Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase.
  J Biol Chem, 281, 37175-37182.
PDB codes: 2huf 2hui 2huu
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.