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Crystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFG
dc.contributor.author | Zhao, Haiyan | |
dc.contributor.author | Tang, Liang | |
dc.date.accessioned | 2015-05-05T20:33:43Z | |
dc.date.available | 2015-05-05T20:33:43Z | |
dc.date.issued | 2009-04-01 | |
dc.identifier.citation | Zhao, H., & Tang, L. (2009). Crystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFG. Acta Crystallografica F Struct Biol Cryst Commun., 64(4), 346-349. http://www.dx.doi.org/10.1107/S174430910900668X | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/17600 | |
dc.description | This is the publisher's version, also available electronically from "http://scripts.iucr.org". | en_US |
dc.description.abstract | YycGF is a highly conserved two-component signal transduction system that is specific to low-G+C Gram-positive bacteria, including many important human pathogens. It has been recognized as a crucial regulatory system for cell-wall metabolism. YycG, the histidine protein kinase of this system, is a multidomain transmembrane protein. The truncated cytoplasmic portion of YycG from Bacillus subtilis encompassing the PAS domain, the dimerization domain and the catalytic domain was expressed, purified and crystallized. X-ray data were collected to 2.8 Å resolution with a completeness of 98.2% and an overall Rmerge of 5.6%. The crystals belonged to space group P61 or P65, with unit-cell parameters a = 135.0, c = 133.0 Å. The selenomethionine-substituted version of the protein was crystallized and X-ray data were collected to 3.6 Å resolution for subsequent MAD phasing. | en_US |
dc.publisher | International Union of Crystallography | en_US |
dc.subject | histidine protein kinases | en_US |
dc.subject | Two-component systems | en_US |
dc.subject | Signal transduction | en_US |
dc.subject | Gram-positive bacteria | en_US |
dc.subject | cell wall | en_US |
dc.subject | PAS domains | en_US |
dc.subject | YycG | en_US |
dc.subject | YycF | en_US |
dc.subject | Autophosphorylation | en_US |
dc.title | Crystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFG | en_US |
dc.type | Article | |
kusw.kuauthor | Tang, Liang | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1107/S174430910900668X | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |