2hqr
From Proteopedia
(New page: 200px<br /><applet load="2hqr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hqr" /> '''Structure of a Atypical Orphan Response Regu...) |
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==Overview== | ==Overview== | ||
| - | Two-component signal transduction systems, commonly found in prokaryotes, typically regulate cellular functions in response to environmental | + | Two-component signal transduction systems, commonly found in prokaryotes, typically regulate cellular functions in response to environmental conditions through a phosphorylation-dependent process. A new type of response regulator, hp1043 (HP-RR) from Helicobacter pylori, has been recently identified. HP-RR is essential for cell growth and does not require the well known phosphorelay scheme. Unphosphorylated HP-RR binds specifically to its own promoter (P(1043)) and autoregulates the promoter of the tlpB gene (P(tlpB)). We have determined the structure of HP-RR by NMR and x-ray crystallography, revealing a symmetrical dimer with two functional domains. The molecular topology resembles that of the OmpR/PhoB subfamily, however, the symmetrical dimer is stable even in the unphosphorylated state. The dimer interface, formed by three secondary structure elements (alpha4-beta5-alpha5), resembles that of the active, phosphorylated forms of ArcA and PhoB. Several conserved residues of the HP-RR dimeric interface deviate from the OmpR/PhoB subfamily, although there are similar salt bridges and hydrophobic patches within the interface. Our findings reveal how a new type of response regulator protein could function as a cell growth-associated regulator in the absence of post-translational modification. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structure of an | + | Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism., Hong E, Lee HM, Ko H, Kim DU, Jeon BY, Jung J, Shin J, Lee SA, Kim Y, Jeon YH, Cheong C, Cho HS, Lee W, J Biol Chem. 2007 Jul 13;282(28):20667-75. Epub 2007 May 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17491010 17491010] |
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: symmetric dimer]] | [[Category: symmetric dimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:40 2008'' |
Revision as of 15:44, 21 February 2008
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Structure of a Atypical Orphan Response Regulator Protein Revealed a New Phosphorylation-Independent Regulatory Mechanism
Overview
Two-component signal transduction systems, commonly found in prokaryotes, typically regulate cellular functions in response to environmental conditions through a phosphorylation-dependent process. A new type of response regulator, hp1043 (HP-RR) from Helicobacter pylori, has been recently identified. HP-RR is essential for cell growth and does not require the well known phosphorelay scheme. Unphosphorylated HP-RR binds specifically to its own promoter (P(1043)) and autoregulates the promoter of the tlpB gene (P(tlpB)). We have determined the structure of HP-RR by NMR and x-ray crystallography, revealing a symmetrical dimer with two functional domains. The molecular topology resembles that of the OmpR/PhoB subfamily, however, the symmetrical dimer is stable even in the unphosphorylated state. The dimer interface, formed by three secondary structure elements (alpha4-beta5-alpha5), resembles that of the active, phosphorylated forms of ArcA and PhoB. Several conserved residues of the HP-RR dimeric interface deviate from the OmpR/PhoB subfamily, although there are similar salt bridges and hydrophobic patches within the interface. Our findings reveal how a new type of response regulator protein could function as a cell growth-associated regulator in the absence of post-translational modification.
About this Structure
2HQR is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism., Hong E, Lee HM, Ko H, Kim DU, Jeon BY, Jung J, Shin J, Lee SA, Kim Y, Jeon YH, Cheong C, Cho HS, Lee W, J Biol Chem. 2007 Jul 13;282(28):20667-75. Epub 2007 May 9. PMID:17491010
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