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PDBsum entry 1gc4

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1gc4
Jmol
Contents
Protein chains
382 a.a. *
Ligands
ASP ×4
PLP ×4
* Residue conservation analysis
PDB id:
1gc4
Name: Transferase
Title: Thermus thermophilus aspartate aminotransferase tetra mutant complexed with aspartate
Structure: Aspartate aminotransferase. Chain: a, b, c, d. Engineered: yes. Mutation: yes
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
3.30Å     R-factor:   0.217     R-free:   0.277
Authors: H.Ura,T.Nakai,K.Hirotsu,S.Kuramitsu
Key ref: H.Ura et al. (2001). Substrate recognition mechanism of thermophilic dual-substrate enzyme. J Biochem, 130, 89-98. PubMed id: 11432784
Date:
19-Jul-00     Release date:   05-Sep-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q56232  (AAT_THET8) -  Aspartate aminotransferase
Seq:
Struc:
385 a.a.
382 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.6.1.1  - Aspartate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-aspartate
Bound ligand (Het Group name = ASP)
corresponds exactly
+ 2-oxoglutarate
= oxaloacetate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     biosynthetic process   1 term 
  Biochemical function     catalytic activity     6 terms  

 

 
    reference    
 
 
J Biochem 130:89-98 (2001)
PubMed id: 11432784  
 
 
Substrate recognition mechanism of thermophilic dual-substrate enzyme.
H.Ura, T.Nakai, S.I.Kawaguchi, I.Miyahara, K.Hirotsu, S.Kuramitsu.
 
  ABSTRACT  
 
Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
15608117 A.P.Dubnovitsky, E.G.Kapetaniou, and A.C.Papageorgiou (2005).
Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus.
  Protein Sci, 14, 97.
PDB codes: 1w23 1w3u
15883191 A.P.Dubnovitsky, R.B.Ravelli, A.N.Popov, and A.C.Papageorgiou (2005).
Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage.
  Protein Sci, 14, 1498-1507.
PDB codes: 2bhx 2bi1 2bi2 2bi3 2bi5 2bi9 2bia 2bie 2big
15889412 K.Hirotsu, M.Goto, A.Okamoto, and I.Miyahara (2005).
Dual substrate recognition of aminotransferases.
  Chem Rec, 5, 160-172.  
14501132 S.Yoshiba, N.Nakagawa, R.Masui, T.Shibata, Y.Inoue, S.Yokoyama, and S.Kuramitsu (2003).
Overproduction, crystallization and preliminary diffraction data of ADP-ribose pyrophosphatase from Thermus thermophilus HB8.
  Acta Crystallogr D Biol Crystallogr, 59, 1840-1842.  
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.