Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-5-1
pubmed:abstractText
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%.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1764
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
839-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Purification and preliminary X-ray crystallographic analysis of the ligand-binding domain of Sinorhizobium meliloti DctB.
pubmed:affiliation
National laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't