2ayy: Difference between revisions
New page: left|200px<br /><applet load="2ayy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ayy" /> '''Solution structure of the E.coli RcsC C-term... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2ayy.gif|left|200px]]<br /><applet load="2ayy" size=" | [[Image:2ayy.gif|left|200px]]<br /><applet load="2ayy" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ayy" /> | caption="2ayy" /> | ||
'''Solution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker region'''<br /> | '''Solution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker region'''<br /> | ||
==Overview== | ==Overview== | ||
The Rcs signalling pathway controls a variety of physiological functions | The Rcs signalling pathway controls a variety of physiological functions like capsule synthesis, cell division or motility in prokaryotes. The Rcs regulation cascade, involving a multi-step phosphorelay between the two membrane-bound hybrid sensor kinases RcsC and RcsD and the global regulator RcsB, is, up to now, one of the most complicated regulatory systems in bacteria. To understand the structural basis of Rcs signal transduction, NMR spectroscopy was employed to determine the solution structure of the RcsC C terminus, possessing a phosphoreceiver domain (RcsC-PR), and a region previously described as a long linker between the histidine kinase domain of RcsC (RcsC-HK) and the RcsC-PR. We have found that the linker region comprises an independent structural domain of a new alpha/beta organization, which we named RcsC-ABL domain (Alpha/Beta/Loop). The ABL domain appears to be a conserved and unique structural element of RcsC-like kinases with no significant sequence homology to other proteins. The second domain of the C terminus, the RcsC-PR domain, represents a well-folded CheY-like phosphoreceiver domain with the central parallel beta-sheet covered with two alpha-helical layers on both sides. We have mapped the interaction of RcsC-ABL and RcsC-PR with the histidine phosphotransfer domain (HPt) of RcsD. In addition we have characterized the interaction with and the conformational effects of Mg2+ and the phosphorylation mimetic BeF(-)(3) on RcsC-ABL and RcsC-PR. | ||
==About this Structure== | ==About this Structure== | ||
2AYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 2AYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYY OCA]. | ||
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: Koglin, A.]] | [[Category: Koglin, A.]] | ||
[[Category: Lohr, F.]] | [[Category: Lohr, F.]] | ||
[[Category: Rogov, V | [[Category: Rogov, V V.]] | ||
[[Category: Rogova, N | [[Category: Rogova, N Y.]] | ||
[[Category: alpha/beta layer]] | [[Category: alpha/beta layer]] | ||
[[Category: new domain]] | [[Category: new domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:29 2008'' | ||
Revision as of 17:32, 21 February 2008
|
Solution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker region
OverviewOverview
The Rcs signalling pathway controls a variety of physiological functions like capsule synthesis, cell division or motility in prokaryotes. The Rcs regulation cascade, involving a multi-step phosphorelay between the two membrane-bound hybrid sensor kinases RcsC and RcsD and the global regulator RcsB, is, up to now, one of the most complicated regulatory systems in bacteria. To understand the structural basis of Rcs signal transduction, NMR spectroscopy was employed to determine the solution structure of the RcsC C terminus, possessing a phosphoreceiver domain (RcsC-PR), and a region previously described as a long linker between the histidine kinase domain of RcsC (RcsC-HK) and the RcsC-PR. We have found that the linker region comprises an independent structural domain of a new alpha/beta organization, which we named RcsC-ABL domain (Alpha/Beta/Loop). The ABL domain appears to be a conserved and unique structural element of RcsC-like kinases with no significant sequence homology to other proteins. The second domain of the C terminus, the RcsC-PR domain, represents a well-folded CheY-like phosphoreceiver domain with the central parallel beta-sheet covered with two alpha-helical layers on both sides. We have mapped the interaction of RcsC-ABL and RcsC-PR with the histidine phosphotransfer domain (HPt) of RcsD. In addition we have characterized the interaction with and the conformational effects of Mg2+ and the phosphorylation mimetic BeF(-)(3) on RcsC-ABL and RcsC-PR.
About this StructureAbout this Structure
2AYY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains., Rogov VV, Rogova NY, Bernhard F, Koglin A, Lohr F, Dotsch V, J Mol Biol. 2006 Nov 17;364(1):68-79. Epub 2006 Jul 29. PMID:17005198
Page seeded by OCA on Thu Feb 21 16:32:29 2008