spacer
spacer

PDBsum entry 1tat

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Aminotransferase PDB id
1tat
Jmol
Contents
Protein chains
401 a.a. *
Ligands
PLP ×2
* Residue conservation analysis
PDB id:
1tat
Name: Aminotransferase
Title: Crystalline mitochondrial aspartate aminotransferase exists two conformations
Structure: Aspartate aminotransferase. Chain: a, b. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Biol. unit: Dimer (from PQS)
Resolution:
3.00Å     R-factor:   0.150    
Authors: E.Hohenester,J.N.Jansonius
Key ref:
E.Hohenester and J.N.Jansonius (1994). Crystalline mitochondrial aspartate aminotransferase exists in only two conformations. J Mol Biol, 236, 963-968. PubMed id: 8120903 DOI: 10.1016/0022-2836(94)90001-9
Date:
04-Oct-93     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00508  (AATM_CHICK) -  Aspartate aminotransferase, mitochondrial
Seq:
Struc:
423 a.a.
401 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 1: E.C.2.6.1.1  - Aspartate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-aspartate
+ 2-oxoglutarate
= oxaloacetate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
   Enzyme class 2: E.C.2.6.1.7  - Kynurenine--oxoglutarate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
L-kynurenine
+ 2-oxoglutarate
= 4-(2-aminophenyl)-2,4-dioxobutanoate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   2 terms 
  Biological process     small molecule metabolic process   9 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
DOI no: 10.1016/0022-2836(94)90001-9 J Mol Biol 236:963-968 (1994)
PubMed id: 8120903  
 
 
Crystalline mitochondrial aspartate aminotransferase exists in only two conformations.
E.Hohenester, J.N.Jansonius.
 
  ABSTRACT  
 
The subunits of the alpha 2-dimeric enzyme aspartate aminotransferase are composed of two distinct domains, one large and one small. The active sites are situated close to both the intersubunit and the interdomain interface. Binding of substrate analogues to the active site induces a large conformational change in the enzyme, whereby the small domain rotates by 13 degrees relative to the large domain and completely buries the ligand. We have determined the crystal structures of chicken mitochondrial aspartate aminotransferase (mAATase) in two new crystal forms. A comparison of the structures of mAATase in five crystal forms, including both the unliganded and the liganded enzyme, shows that mAATase exists in either one of two unique conformations, with only minimal adaptations to the crystal lattice. This suggests that both the open, unliganded and closed, liganded structure of mAATase are, to a large extent, stabilized by intramolecular interactions, and are consequently representative of functional states of the protein in solution. A 2-fold-symmetric packing interaction between small domains occurring identically in three crystal forms of mAATase is described.
 
  Selected figure(s)  
 
Figure 2.
igure 2. '-difference plots for the OPI-CLI. OP2-OPI. (X2-c'L1 and the C'LY-(`LI superpositions. One subunit of thr dimer is represented by thick lines. the other one by thin lines. The respective r.m.s. deviations rr I+!). 0.36. (b and 31 or all 802 Y-atoms, and @39, 027. 0% and 0.29 A for the Y-atnms of only thr large domains (residues WA to 258 and residues 48B to 325B). The structures were superimposed as for Figure i.
Figure 3.
Figure 3. The f-fold-symmetric packing contact. observed in he `LI, L3 and OP2 crystals. One small domain of the mAATase dimer is repreented with thick lines, and the small domain of an adjacent dimer is represented with thin lines. The 2-fold symmety xis shown orresponds o a rystallographic dyad in the (`Ll crystals. but is local in (`I,3 and OP.) crystals.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1994, 236, 963-968) copyright 1994.  

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
15103612 Y.Katsura, M.Shirouzu, H.Yamaguchi, R.Ishitani, O.Nureki, S.Kuramitsu, H.Hayashi, and S.Yokoyama (2004).
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV.
  Proteins, 55, 487-492.
PDB code: 1iug
11807243 T.R.Schneider (2002).
A genetic algorithm for the identification of conformationally invariant regions in protein molecules.
  Acta Crystallogr D Biol Crystallogr, 58, 195-208.  
9188741 A.V.Efimov (1997).
Structural trees for protein superfamilies.
  Proteins, 28, 241-260.  
9083108 M.Bergdoll, M.H.Remy, C.Cagnon, J.M.Masson, and P.Dumas (1997).
Proline-dependent oligomerization with arm exchange.
  Structure, 5, 391-401.  
8665890 Z.Marković-Housley, T.Schirmer, E.Hohenester, A.R.Khomutov, R.M.Khomutov, M.Y.Karpeisky, E.Sandmeier, P.Christen, and J.N.Jansonius (1996).
Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase.
  Eur J Biochem, 236, 1025-1032.
PDB codes: 1oxo 1oxp
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.