2hqo

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[[Image:2hqo.jpg|left|200px]]
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{{STRUCTURE_2hqo| PDB=2hqo | SCENE= }}
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|RELATEDENTRY=[[2hqn|2HQN]], [[2hqr|2HQR]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hqo OCA], [http://www.ebi.ac.uk/pdbsum/2hqo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hqo RCSB]</span>
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'''Structure of a Atypical Orphan Response Regulator Protein Revealed a New Phosphorylation-Independent Regulatory Mechanism'''
'''Structure of a Atypical Orphan Response Regulator Protein Revealed a New Phosphorylation-Independent Regulatory Mechanism'''
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[[Category: Hong, E.]]
[[Category: Hong, E.]]
[[Category: Lee, W.]]
[[Category: Lee, W.]]
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[[Category: phosporylation-independent response regulator]]
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[[Category: Phosporylation-independent response regulator]]
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[[Category: regulatory domain]]
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[[Category: Regulatory domain]]
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[[Category: symmetric dimer]]
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[[Category: Symmetric dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:35:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:34:02 2008''
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Revision as of 03:35, 4 May 2008

Template:STRUCTURE 2hqo

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

2HQO 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 Page seeded by OCA on Sun May 4 06:35:40 2008

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