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TitleConformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis
Journal, issue, pagesJ. BIOL. CHEM., Vol. 278, Page 9481-9488, Year 2003
Publish dateJun 14, 2002 (structure data deposition date)
AuthorsHayashi, H. / Mizuguchi, H. / Miyahara, I. / Nakajima, Y. / Hirotsu, K. / Kagamiyama, H.
External linksJ. BIOL. CHEM. / PubMed:12488449
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-1ix6:
Aspartate Aminotransferase Active Site Mutant V39F
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1ix7:
Aspartate Aminotransferase Active Site Mutant V39F maleate complex
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1ix8:
Aspartate Aminotransferase Active Site Mutant V39F/N194A
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-MAE:
MALEIC ACID

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / ACTIVE SITE MUTANT

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