2hqo: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:2hqo.jpg|left|200px]]
{{Seed}}
[[Image:2hqo.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hqo|  PDB=2hqo  |  SCENE=  }}  
{{STRUCTURE_2hqo|  PDB=2hqo  |  SCENE=  }}  


'''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===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_17491010}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17491010 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17491010}}


==About this Structure==
==About this Structure==
2HQO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQO OCA].  
2HQO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQO OCA].  


==Reference==
==Reference==
Line 27: Line 31:
[[Category: Regulatory domain]]
[[Category: Regulatory domain]]
[[Category: Symmetric dimer]]
[[Category: Symmetric dimer]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:35:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:39:53 2008''

Revision as of 08:39, 29 July 2008

File:2hqo.png

Template:STRUCTURE 2hqo

Structure of a Atypical Orphan Response Regulator Protein Revealed a New Phosphorylation-Independent Regulatory Mechanism

Template:ABSTRACT PUBMED 17491010

About this Structure

2HQO is a Single protein structure of sequence from Helicobacter pylori. Full experimental 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 Tue Jul 29 11:39:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2hqo&oldid=739608"