2hqn

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(New page: 200px<br /><applet load="2hqn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hqn" /> '''Structure of a Atypical Orphan Response Regu...)
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==Overview==
==Overview==
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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.
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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==
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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]
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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: phosporylation-independent response regulator]]
[[Category: phosporylation-independent response regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:22:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:39 2008''

Revision as of 15:44, 21 February 2008


2hqn

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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

2HQN 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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