Purification and preliminary X-ray crystallographic analysis of the ligand-binding domain of Sinorhizobium meliloti DctB.

abstract

• Sinorhizobium meliloti DctBD is a well-characterized two-component system. It is believed that DctB senses the concentration of C4-dicarboxylate compounds on the outside of the bacterium and phosphorylates DctD, which in turn activates transcription of the dctA gene, coding for a gene of C4-dicarboxylate permease. The structure and function of the ligand-binding domain of DctB has not been thoroughly investigated. In this study, this domain was produced in E. coli in soluble form, and purified to homogeneity. Crystals were obtained by hanging-drop vapor-diffusion method. The crystals diffracted to 2.3 A resolution and belonged to P42 space group with unit cell dimensions of a = b = 71.77 A, c = 227.14 A. The asymmetric unit contains four molecules with a corresponding VM of 2.4 A3 Da(-1) and a solvent content of 49.1%.

authors

• Nan, Beiyan

published proceedings

• Biochim Biophys Acta

author list (cited authors)

• Nan, B., Zhou, Y., Liang, Y., Wen, J., Ma, Q. i., Zhang, S., Wang, Y., & Su, X.

citation count

• 6

complete list of authors

• Nan, Beiyan||Zhou, Yanfeng||Liang, Yu-He||Wen, Jin||Ma, Qi||Zhang, Siwei||Wang, Yiping||Su, Xiao-Dong

publication date

• April 2006

publisher

• Elsevier  Publisher

published in

• Biochimica et Biophysica Acta: international journal of biochemistry and biophysics  Journal

keywords

• Bacterial Proteins
• Crystallography, X-Ray
• Dicarboxylic Acid Transporters
• Ligands
• Protein Binding
• Sinorhizobium Meliloti

PubMed Central ID

• 16332458

Digital Object Identifier (DOI)

• 10.1016/j.bbapap.2005.10.023

start page

• 839

end page

• 841

volume

• 1764

issue

• 4

URL

• http://dx.doi.org/10.1016/j.bbapap.2005.10.023