2rnj: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2rnj.jpg|left|200px]]
{{Seed}}
[[Image:2rnj.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rnj|  PDB=2rnj  |  SCENE=  }}  
{{STRUCTURE_2rnj|  PDB=2rnj  |  SCENE=  }}  


'''NMR Structure of The S. Aureus VraR DNA Binding Domain'''
===NMR Structure of The S. Aureus VraR DNA Binding Domain===




==Overview==
<!--
In Staphylococcus aureus, a two-component signaling system consisting of the histidine kinase VraS and the response regulator VraR stimulates gene expression in response to antibiotics that inhibit cell wall formation. With respect to understanding the mechanism of the VraSR response and precise interaction of VraR at promoter sites, the structure of the VraR DNA binding domain (DBD) was determined using NMR methods. The DBD demonstrates a four-helix configuration that is shared with the NarL/FixJ family of response regulators and is monomeric in solution. Unobservable amide resonances in VraR NMR spectra coincided with a set of DNA backbone contact sites predicted from a model of a VraR-DNA complex. This observation suggests that a degree of conformational sampling is required to achieve a high-affinity interaction with DNA. On the basis of chemical shift differences and line broadening, an amino-terminal 3 10 helix and a portion of helix H4 identify a continuous surface that may link the DBD to the receiver domain. The full-length VraR protein thermally denatured with a single transition, suggesting that the receiver domain and DBD were integrated and not simply tethered. Of note, the DBD alone denatured at a temperature that was 21 degrees C higher than that of the full-length protein. Thus, the DBD appears to be thermodynamically and structurally sensitive to state of the receiver domain.
The line below this paragraph, {{ABSTRACT_PUBMED_18293926}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18293926 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18293926}}


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


==Reference==
==Reference==
Line 34: Line 38:
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Two-component regulatory system]]
[[Category: Two-component regulatory system]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:13:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:21:54 2008''

Revision as of 05:21, 28 July 2008

File:2rnj.png

Template:STRUCTURE 2rnj

NMR Structure of The S. Aureus VraR DNA Binding Domain

Template:ABSTRACT PUBMED 18293926

About this Structure

2RNJ is a Single protein structure of sequence from Staphylococcus aureus. Full experimental information is available from OCA.

Reference

The NMR Structure of the Staphylococcus aureus Response Regulator VraR DNA Binding Domain Reveals a Dynamic Relationship between It and Its Associated Receiver Domain., Donaldson LW, Biochemistry. 2008 Mar 18;47(11):3379-88. Epub 2008 Feb 23. PMID:18293926

Page seeded by OCA on Mon Jul 28 08:21:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2rnj&oldid=689684"