Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Shao Yang Ku"'
Autor:
Shao-Yang Ku1,2 syku@sickkids.ca, Cornell, Kenneth A.3 kencornell@boisestate.edu, Howell, P. Lynne1,2 howell@sickkids.ca
Publikováno v:
BMC Structural Biology. 2007, Vol. 7, p70-82. 13p.
Publikováno v:
Acta Crystallographica: Section D (Wiley-Blackwell). Jul2006, Vol. 62 Issue 7, p814-823. 10p. 4 Diagrams, 1 Chart, 1 Graph.
Autor:
Shao Yang Ku, Jean-Bernard Behr, P. Lynne Howell, Kenneth A. Cornell, Patrick Yip, Georges Guillerm, Michael K. Riscoe
Publikováno v:
Journal of Biological Chemistry. 282:22195-22206
The methionine salvage pathway is ubiquitous in all organisms, but metabolic variations exist between bacteria and mammals. 5-Methylthioribose (MTR) kinase is a key enzyme in methionine salvage in bacteria and the absence of a mammalian homolog sugge
Publikováno v:
Nature Structural Biology. 7:287-291
Siderophore binding proteins play a key role in the uptake of iron in many gram-positive and gram-negative bacteria. FhuD is a soluble periplasmic binding protein that transports ferrichrome and other hydroxamate siderophores. The crystal structure o
Autor:
Jason Koo, Shao-Yang Ku, Lori L. Burrows, Liliana M. Sampaleanu, Stephanie Tammam, P. Lynne Howell
Type IV pili (T4P) are retractile appendages that contribute to the virulence of bacterial pathogens. PilF is a Pseudomonas aeruginosa lipoprotein that is essential for T4P biogenesis. Phenotypic characterization of a pilF mutant confirmed that T4P-m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::429eb91f2c18624ed9fe2b78997d3acf
https://europepmc.org/articles/PMC2580691/
https://europepmc.org/articles/PMC2580691/
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 63(Pt 4)
Trivalent holmium ions were shown to isomorphously replace magnesium ions to form an ADP-2Ho complex in the nucleotide-binding domain of Bacillus subtilis 5-methylthioribose (MTR) kinase. This nucleotide-holmium complex provided sufficient phasing po
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 62(Pt 7)
Pyridoxal 5'-phosphate (PLP) dependent tryptophanase has been isolated from Escherichia coli and its crystal structure has been determined. The structure shares the same fold with and has similar quaternary structure to Proteus vulgaris tryptophanase
Autor:
Thomas R. Schneider, Shao-Yang Ku
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 65:s160-s161
Autor:
Shao-Yang Ku, Thomas R. Schneider
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 66:s315-s315
Publikováno v:
BMC Structural Biology
BMC Structural Biology, Vol 7, Iss 1, p 70 (2007)
BMC Structural Biology, Vol 7, Iss 1, p 70 (2007)
Background Metabolic variations exist between the methionine salvage pathway of humans and a number of plants and microbial pathogens. 5-Methylthioribose (MTR) kinase is a key enzyme required for methionine salvage in plants and many bacteria. The ab