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A preliminary X-ray study of a refolded PTS EIIBfruc protein from Escherichia coli

Title
A preliminary X-ray study of a refolded PTS EIIBfruc protein from Escherichia coli
Authors
Shin D.H.
Ewha Authors
신동해
SCOPUS Author ID
신동해scopus
Issue Date
2008
Journal Title
Protein and Peptide Letters
ISSN
0929-8665JCR Link
Citation
vol. 15, no. 6, pp. 630 - 632
Indexed
SCIE; SCOPUS WOS scopus
Abstract
The phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) catalyzes the phosphorylation and transportation of its sugar substrates. A sugar-specific enzyme II complex involved in the PTS finally functions to translocate substrates across the membrane. A PTS EIIBfruc protein, a fructose specific EIIB subunit, from Escherichia coli has been cloned, expressed, refolded, purified, and crystallized. The synchrotron data were collected to 2.6 Å from the crystal of a selenomethionine substitute PTS EIIBfruc protein. The crystal belongs to the primitive trigonal space group P3121, with unit-cell parameters of a = 33.4 Å, b = 33.4 Å, c = 154.0 Å, and β = 120.0°. A full structure determination is under way to provide insights into the structure-function relationships of this protein. © 2008 Bentham Science Publishers Ltd.
DOI
10.2174/092986608784967001
Appears in Collections:
약학대학 > 약학과 > Journal papers
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