2BFN
The crystal structure of the complex of the haloalkane dehalogenase LinB with the product of dehalogenation reaction 1,2-dichloropropane.
Summary for 2BFN
Entry DOI | 10.2210/pdb2bfn/pdb |
Related | 1CV2 1D07 1G42 1G4H 1G5F 1IZ7 1IZ8 1K5P 1K63 1K6E 1MJ5 |
Descriptor | HALOGENALKANE DEHALOGENASE, (2S)-2,3-DICHLOROPROPAN-1-OL, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | haloalkane dehalogenase linb, 1\, 2\, 3-trichloropropane, hydrolase, alpha/beta-hydrolase |
Biological source | SPHINGOMONAS PAUCIMOBILIS |
Cellular location | Periplasm: P51698 |
Total number of polymer chains | 1 |
Total formula weight | 33429.28 |
Authors | Banas, P.,Otyepka, M.,Jerabek, P.,Vevodova, J.,Bohac, M.,Damborsky, J. (deposition date: 2004-12-09, release date: 2006-06-26, Last modification date: 2023-12-13) |
Primary citation | Minincova, M.,Prokop, Z.,Vevodova, J.,Nagata, Y.,Damborsky, J. Weak Activity of Haloalkane Dehalogenase Linb with 1,2,3-Trichloropropane Revealed by X-Ray Crystallography and Microcalorimetry Appl.Environ.Microbiol., 73:2005-, 2007 Cited by PubMed Abstract: 1,2,3-Trichloropropane (TCP) is a highly toxic and recalcitrant compound. Haloalkane dehalogenases are bacterial enzymes that catalyze the cleavage of a carbon-halogen bond in a wide range of organic halogenated compounds. Haloalkane dehalogenase LinB from Sphingobium japonicum UT26 has, for a long time, been considered inactive with TCP, since the reaction cannot be easily detected by conventional analytical methods. Here we demonstrate detection of the weak activity (k(cat) = 0.005 s(-1)) of LinB with TCP using X-ray crystallography and microcalorimetry. This observation makes LinB a useful starting material for the development of a new biocatalyst toward TCP by protein engineering. Microcalorimetry is proposed to be a universal method for the detection of weak enzymatic activities. Detection of these activities is becoming increasingly important for engineering novel biocatalysts using the scaffolds of proteins with promiscuous activities. PubMed: 17259360DOI: 10.1128/AEM.02416-06 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
