1gd9
From Proteopedia
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CRYSTALL STRUCTURE OF PYROCOCCUS PROTEIN-A1
Overview
We determined the crystal structure of the liganded form of, alpha-aminotransferase from a hyperthermophile, Pyrococcus horikoshii., This hyperthermophilic enzyme did not show domain movement upon binding of, an acidic substrate, glutamate, except for a small movement of the, alpha-helix from Glu16 to Ala25. The omega-carboxyl group of the acidic, substrate was recognized by Tyr70* without its side-chain movement, but, not by positively charged Arg or Lys. Compared with the homologous enzymes, from Thermus thermophilus HB8 and Escherichia coli, it was suggested that, the more thermophilic the enzyme is, the smaller the domain movement is., This rule seems to be applicable to many other enzymes already reported.
About this Structure
1GD9 is a Single protein structure of sequence from Pyrococcus horikoshii with PLP as ligand. Full crystallographic information is available from OCA.
Reference
Temperature dependence of the enzyme-substrate recognition mechanism., Ura H, Harata K, Matsui I, Kuramitsu S, J Biochem (Tokyo). 2001 Jan;129(1):173-8. PMID:11134972
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