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TitleCrystal Structure of DmdD, a Crotonase Superfamily Enzyme That Catalyzes the Hydration and Hydrolysis of Methylthioacryloyl-CoA.
Journal, issue, pagesPlos One, Vol. 8, Page e63870-e63870, Year 2013
Publish dateJan 29, 2013 (structure data deposition date)
AuthorsTan, D. / Crabb, W.M. / Whitman, W.B. / Tong, L.
External linksPlos One / PubMed:23704947
MethodsX-ray diffraction
Resolution1.504 - 1.8 Å
Structure data

PDB-4izb:
Crystal structure of DmdD, a crotonase superfamily enzyme that catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 1.504 Å

PDB-4izc:
Crystal structure of DmdD E121A in complex with MTA-CoA
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4izd:
Crystal structure of DmdD E121A in complex with MMPA-CoA
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-1GZ:
methylthioacryloyl-CoA

ChemComp-1HE:
3-methylmercaptopropionate-CoA (MMPA-CoA)

Source
  • ruegeria pomeroyi (bacteria)
KeywordsHYDROLASE / ENOYL-COA HYDRATASE / Dimethyl-sulphoniopropionate (DMSP) METABOLISM / methylthioacryloyl-CoA (MTA-CoA) / CROTONASE FOLD / hydrolase/substrate / ENYOL-COA HYDRATASE / hydrolase-hydrolase inhibitor complex / hydrolase-substrate complex

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