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Structure paper

TitleA conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding.
Journal, issue, pagesBiochemistry, Vol. 50, Page 2357-2363, Year 2011
Publish dateDec 15, 2009 (structure data deposition date)
AuthorsLight, S.H. / Minasov, G. / Shuvalova, L. / Peterson, S.N. / Caffrey, M. / Anderson, W.F. / Lavie, A.
External linksBiochemistry / PubMed:21291284
MethodsX-ray diffraction
Resolution1.03 - 1.9 Å
Structure data

PDB-3l2i:
1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium LT2.
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3o1n:
1.03 Angstrom Crystal Structure of Q236A Mutant Type I Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium
Method: X-RAY DIFFRACTION / Resolution: 1.03 Å

PDB-3oex:
Crystal Structure of Type I 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium with close loop conformation.
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • salmonella enterica subsp. enterica serovar typhimurium (bacteria)
KeywordsLYASE / 3-dehydroquinate dehydratase / aroD / Shikimate pathway / idp90922 / csgid / Amino-acid biosynthesis / Aromatic amino acid biosynthesis / Schiff base / Structural Genomics / Center for Structural Genomics of Infectious Diseases / TIM barrel / dehydratase

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