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TitleKinetic, Mutational, and Structural Analysis of Malonate Semialdehyde Decarboxylase from Coryneform Bacterium Strain FG41: Mechanistic Implications for the Decarboxylase and Hydratase Activities.
Journal, issue, pagesBiochemistry, Vol. 52, Page 4830-4841, Year 2013
Publish dateApr 13, 2010 (structure data deposition date)
AuthorsGuo, Y. / Serrano, H. / Poelarends, G.J. / Johnson, W.H. / Hackert, M.L. / Whitman, C.P.
External linksBiochemistry / PubMed:23781927
MethodsX-ray diffraction
Resolution2.02 - 2.4 Å
Structure data

PDB-3mjz:
The crystal structure of native FG41 MSAD
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3mlc:
Crystal structure of FG41MSAD inactivated by 3-chloropropiolate
Method: X-RAY DIFFRACTION / Resolution: 2.224 Å

PDB-4lho:
Crystal Structure of FG41Malonate Semialdehyde Decarboxylase inhibited by 3-bromopropiolate
Method: X-RAY DIFFRACTION / Resolution: 2.224 Å

PDB-4lhp:
Crystal Structure of Native FG41Malonate Semialdehyde Decarboxylase
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PR6:
3-chloro-3-oxopropanoic acid

ChemComp-PO4:
PHOSPHATE ION

ChemComp-SO4:
SULFATE ION

Source
  • coryneform bacterium (bacteria)
KeywordsISOMERASE / The tautomerase superfamily / Malonate Semialdehyde Decarboxylase / Beta-alpha-beta-motif / Tautomerase superfamily / Coryneform bacterium FG41 / ISOMERASE/ISOMERASE INHIBITOR / ISOMERASE-ISOMERASE INHIBITOR complex

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