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Structure paper

TitleThe X-ray structure of trans-3-chloroacrylic acid dehalogenase reveals a novel hydration mechanism in the tautomerase superfamily
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 11546-11552, Year 2004
Publish dateJan 5, 2004 (structure data deposition date)
Authorsde Jong, R.M. / Brugman, W. / Poelarends, G.J. / Whitman, C.P. / Dijkstra, B.W.
External linksJ. Biol. Chem. / PubMed:14701869
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-1s0y:
The structure of trans-3-chloroacrylic acid dehalogenase, covalently inactivated by the mechanism-based inhibitor 3-bromopropiolate at 2.3 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-MLA:
MALONIC ACID

ChemComp-HOH:
WATER

Source
  • pseudomonas pavonaceae (bacteria)
KeywordsLYASE / dehalogenase / tautomerase family / covalent modification / inhibition / Michael addition / dehalogenation mechanism / malonyl inhibitor

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