Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
19342778
PubMed Central
PMC2664758
DOI
10.1107/s1744309109007039
PII: S1744309109007039
Knihovny.cz E-zdroje
- MeSH
- Bradyrhizobium enzymologie MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- hydrolasy chemie MeSH
- krystalizace MeSH
- krystalografie rentgenová MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- haloalkane dehalogenase MeSH Prohlížeč
- hydrolasy MeSH
A novel enzyme, DbeA, belonging to the haloalkane dehalogenase family (EC 3.8.1.5) was isolated from Bradyrhizobium elkani USDA94. This haloalkane dehalogenase is closely related to the DbjA enzyme from B. japonicum USDA110 (71% sequence identity), but has different biochemical properties. DbeA is generally less active and has a higher specificity towards brominated and iodinated compounds than DbjA. In order to understand the altered activity and specificity of DbeA, its mutant variant DbeA1, which carries the unique fragment of DbjA, was also constructed. Both wild-type DbeA and DbeA1 were crystallized using the sitting-drop vapour-diffusion method. The crystals of DbeA belonged to the primitive orthorhombic space group P2(1)2(1)2(1), while the crystals of DbeA1 belonged to the monoclinic space group C2. Diffraction data were collected to 2.2 A resolution for both DbeA and DbeA1 crystals.
Zobrazit více v PubMed
Chovancová, E., Kosinski, J., Bujnicki, J. M. & Damborský, J. (2007). Proteins, 67, 305–316. PubMed
Ducruix, A. & Giegé, R. (1999). Crystallization of Nucleic Acids and Proteins. A Practical Approach, 2nd ed. Oxford University Press.
Ikeda-Ohtsubo, W., Goto, Y., Sato, Y., Ohtsubo, Y., Minamisawa, K., Tsuda, M., Damborský, J. & Nagata, Y. (2009). In preparation.
Janssen, D. B., Dinkla, I. J. T., Poelarends, G. J. & Terpstra, P. (2005). Environ. Microbiol.7, 1868–1882. PubMed
Jesenská, A., Pavlová, M., Strouhal, M., Chaloupková, R., Těšínska, I., Monincová, M., Prokop, Z., Bartoš, M., Pavlík, I., Rychlík, I., Möbius, P., Nagata, Y. & Damborský, J. (2005). Appl. Environ. Microbiol.71, 6736–6745. PubMed PMC
Kabsch, W. (1993). J. Appl. Cryst.26, 795–800.
Kulakova, A. N., Larkin, M. J. & Kulakov, L. A. (1997). Microbiology, 143, 109–115. PubMed
Marek, J., Vévodová, J., Smatanová, I. K., Nagata, Y., Svensson, L. A., Newman, J., Takagi, M. & Damborský, J. (2000). Biochemistry39, 14082–14086. PubMed
Mazumdar, P. A., Hulecki, J. C., Cherney, M. M., Garen, C. R. & James, M. N. (2008). Biochim. Biophys. Acta, 1784, 351–362. PubMed
Minor, W., Cymborowski, M., Otwinowski, Z. & Chruszcz, M. (2006). Acta Cryst. D62, 859–866. PubMed
Mozga, T., Sato, Y., Chaloupková, R., Koudelaková, T., Nagata, Y. & Damborský, J. (2009). In preparation.
Nagata, Y., Hynková, K., Damborský, J. & Takagi, M. (1999). Protein Expr. Purif.17, 299–304. PubMed
Nagata, Y., Miyauchi, K., Damborsky, J., Manova, K., Ansorgova, A. & Takagi, M. (1997). Appl. Environ. Microbiol.63, 3707–3710. PubMed PMC
Newman, J., Peat, T. S., Richard, R., Kan, L., Swanson, P. E., Affholter, J. A., Holmes, I. H., Schindler, J. F., Unkefer, C. J. & Terwilliger, T. C. (1999). Biochemistry, 38, 16105–16114. PubMed
Prokop, Z., Damborsky, J., Nagata, Y. & Janssen, D. B. (2004). Patent WO 2006/079295 A2.
Prokop, Z., Damborsky, J., Oplustil, F., Jesenska, A. & Nagata, Y. (2005). Patent WO 2006/128390 A1.
Sato, Y., Monincová, M., Chaloupková, R., Prokop, Z., Ohtsubo, Y., Minamisawa, K., Tsuda, M., Damborský, J. & Nagata, Y. (2005). Appl. Environ. Microbiol.71, 4372–4379. PubMed PMC
Sato, Y., Natsume, R., Tsuda, M., Damborsky, J., Nagata, Y. & Senda, T. (2007). Acta Cryst. F63, 294–296. PubMed PMC
Stsiapanava, A., Koudelakova, T., Lapkouski, M., Pavlova, M., Damborsky, J. & Kuta Smatanova, I. (2008). Acta Cryst. F64, 137–140. PubMed PMC
Swanson, P. E. (1999). Curr. Opin. Biotechnol.10, 365–369. PubMed