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TitleEvolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans.
Journal, issue, pagesBiochemistry, Vol. 46, Page 12896-12908, Year 2007
Publish dateJul 7, 2007 (structure data deposition date)
AuthorsRakus, J.F. / Fedorov, A.A. / Fedorov, E.V. / Glasner, M.E. / Vick, J.E. / Babbitt, P.C. / Almo, S.C. / Gerlt, J.A.
External linksBiochemistry / PubMed:17944491
MethodsX-ray diffraction
Resolution1.8 - 2.2 Å
Structure data

PDB-2qjj:
Crystal structure of D-Mannonate dehydratase from Novosphingobium aromaticivorans
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2qjm:
Crystal structure of the K271E mutant of Mannonate dehydratase from Novosphingobium aromaticivorans complexed with Mg and D-mannonate
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2qjn:
Crystal structure of D-mannonate dehydratase from Novosphingobium aromaticivorans complexed with Mg and 2-keto-3-deoxy-D-gluconate
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CS2:
D-MANNONIC ACID

ChemComp-KDG:
2-KETO-3-DEOXYGLUCONATE

Source
  • novosphingobium aromaticivorans (bacteria)
KeywordsLYASE / Mannonate dehydratase / Enolase superfamily / D-mannonate dehydratase

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