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PDBsum entry 1gtx

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1gtx
Jmol
Contents
Protein chains
462 a.a.
Ligands
ACT ×4
PLP ×4
Waters ×52
Superseded by: 1ohv 1ohv
PDB id:
1gtx
Name: Transferase
Title: 4-aminobutyrate-aminotransferase from pig
Structure: 4-aminobutyrate aminotransferase. Chain: a, b, c, d. Synonym: gaba-at. Ec: 2.6.1.19
Source: Sus scrofa. Pig. Organ: liver. Organelle: mitochondria. Cellular_location: intramitochondrial
Biol. unit: Dimer (from PQS)
Resolution:
3.00Å     R-factor:   0.186     R-free:   0.217
Authors: P.Storici,G.Capitani,T.Schirmer
Key ref:
P.Storici et al. (1999). Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy. Biochemistry, 38, 8628-8634. PubMed id: 10393538 DOI: 10.1021/bi990478j
Date:
04-Feb-99     Release date:   04-Feb-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P80147  (GABT_PIG) -  4-aminobutyrate aminotransferase, mitochondrial
Seq:
Struc:
500 a.a.
462 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.6.1.19  - 4-aminobutyrate--2-oxoglutarate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
4-aminobutanoate
+ 2-oxoglutarate
= succinate semialdehyde
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1021/bi990478j Biochemistry 38:8628-8634 (1999)
PubMed id: 10393538  
 
 
Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy.
P.Storici, G.Capitani, D.De Biase, M.Moser, R.A.John, J.N.Jansonius, T.Schirmer.
 
  ABSTRACT  
 
gamma-Aminobutyrate aminotransferase (GABA-AT), a pyridoxal phosphate-dependent enzyme, is responsible for the degradation of the inhibitory neurotransmitter GABA and is a target for antiepileptic drugs because its selective inhibition raises GABA concentrations in brain. The X-ray structure of pig GABA-AT has been determined to 3.0 A resolution by molecular replacement with the distantly related enzyme ornithine aminotransferase. Both omega-aminotransferases have the same fold, but exhibit side chain replacements in the closely packed binding site that explain their respective specificities. The aldimines of GABA and the antiepileptic drug vinyl-GABA have been modeled into the active site.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18846220 F.Ludewig, A.Hüser, H.Fromm, L.Beauclair, and N.Bouché (2008).
Mutants of GABA transaminase (POP2) suppress the severe phenotype of succinic semialdehyde dehydrogenase (ssadh) mutants in Arabidopsis.
  PLoS ONE, 3, e3383.  
  19513195 J.Stránská, D.Kopecný, M.Tylichová, J.Snégaroff, and M.Sebela (2008).
Ornithine delta-aminotransferase: An enzyme implicated in salt tolerance in higher plants.
  Plant Signal Behav, 3, 929-935.  
17988865 M.D.Clift, and R.B.Silverman (2008).
Synthesis and evaluation of novel aromatic substrates and competitive inhibitors of GABA aminotransferase.
  Bioorg Med Chem Lett, 18, 3122-3125.  
17680699 V.Rajaram, P.Ratna Prasuna, H.S.Savithri, and M.R.Murthy (2008).
Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: studies on substrate specificity and inhibitor binding.
  Proteins, 70, 429-441.
PDB codes: 2pb0 2pb2
17355287 G.Andersen, B.Andersen, D.Dobritzsch, K.D.Schnackerz, and J.Piskur (2007).
A gene duplication led to specialized gamma-aminobutyrate and beta-alanine aminotransferase in yeast.
  FEBS J, 274, 1804-1817.  
16632251 L.Bai, L.Li, H.Xu, K.Minagawa, Y.Yu, Y.Zhang, X.Zhou, H.G.Floss, T.Mahmud, and Z.Deng (2006).
Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A.
  Chem Biol, 13, 387-397.  
  17012789 V.Rajaram, K.Prasad, P.Ratna Prasuna, N.Ramachandra, S.R.Bharath, H.S.Savithri, and M.R.Murthy (2006).
Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the biosynthetic N-acetylornithine aminotransferases from Salmonella typhimurium and Escherichia coli.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 980-983.  
16096275 M.Markova, C.Peneff, M.J.Hewlins, T.Schirmer, and R.A.John (2005).
Determinants of substrate specificity in omega-aminotransferases.
  J Biol Chem, 280, 36409-36416.
PDB codes: 2byj 2byl
15189147 A.C.Eliot, and J.F.Kirsch (2004).
Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
  Annu Rev Biochem, 73, 383-415.  
15498941 A.Paiardini, F.Bossa, and S.Pascarella (2004).
Evolutionarily conserved regions and hydrophobic contacts at the superfamily level: The case of the fold-type I, pyridoxal-5'-phosphate-dependent enzymes.
  Protein Sci, 13, 2992-3005.  
15150739 N.E.Preece, J.Houseman, M.D.King, R.O.Weller, and S.R.Williams (2004).
Development of vigabatrin-induced lesions in the rat brain studied by magnetic resonance imaging, histology, and immunocytochemistry.
  Synapse, 53, 36-43.  
14534310 P.Storici, D.De Biase, F.Bossa, S.Bruno, A.Mozzarelli, C.Peneff, R.B.Silverman, and T.Schirmer (2004).
Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin.
  J Biol Chem, 279, 363-373.
PDB codes: 1ohv 1ohw 1ohy
10673430 G.Schneider, H.Käck, and Y.Lindqvist (2000).
The manifold of vitamin B6 dependent enzymes.
  Structure, 8, R1-R6.  
10951220 S.G.Jeon, J.H.Bahn, J.S.Jang, J.Park, O.S.Kwon, S.W.Cho, and S.Y.Choi (2000).
Human brain GABA transaminase tissue distribution and molecular expression.
  Eur J Biochem, 267, 5601-5607.  
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 codes are shown on the right.