1je8: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1je8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1je8, resolution 2.12Å" /> '''Two-Component respon...
 
No edit summary
Line 1: Line 1:
[[Image:1je8.gif|left|200px]]<br /><applet load="1je8" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1je8.gif|left|200px]]<br /><applet load="1je8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1je8, resolution 2.12&Aring;" />
caption="1je8, resolution 2.12&Aring;" />
'''Two-Component response regulator NarL/DNA Complex: DNA Bending Found in a High Affinity Site'''<br />
'''Two-Component response regulator NarL/DNA Complex: DNA Bending Found in a High Affinity Site'''<br />


==Overview==
==Overview==
Two-component signal transduction systems are modular phosphorelay, regulatory pathways common in prokaryotes. In the co-crystal structure of, the Escherichia coli NarL signal output domain bound to DNA, we observe, how the NarL family of two-component response regulators can bind DNA. DNA, recognition is accompanied by the formation of a new dimerization, interface, which could occur only in the full-length protein via a large, intramolecular domain rearrangement. The DNA is recognized by the, concerted effects of solvation, van der Waals forces and inherent DNA, deformability, rather than determined primarily by major groove hydrogen, bonding. These subtle forces permit a small DNA-binding domain to perturb, the DNA helix, leading to major DNA curvature and a transition from B- to, A-form DNA at the binding site, where valine on the recognition helix, interacts unexpectedly with the polar major groove floor.
Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component response regulators can bind DNA. DNA recognition is accompanied by the formation of a new dimerization interface, which could occur only in the full-length protein via a large intramolecular domain rearrangement. The DNA is recognized by the concerted effects of solvation, van der Waals forces and inherent DNA deformability, rather than determined primarily by major groove hydrogen bonding. These subtle forces permit a small DNA-binding domain to perturb the DNA helix, leading to major DNA curvature and a transition from B- to A-form DNA at the binding site, where valine on the recognition helix interacts unexpectedly with the polar major groove floor.


==About this Structure==
==About this Structure==
1JE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JE8 OCA].  
1JE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JE8 OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bearson, S.M.D.]]
[[Category: Bearson, S M.D.]]
[[Category: Dickerson, R.E.]]
[[Category: Dickerson, R E.]]
[[Category: Gunsalus, R.P.]]
[[Category: Gunsalus, R P.]]
[[Category: Jarvis, M.R.]]
[[Category: Jarvis, M R.]]
[[Category: Kaczor-Grzeskowiak, M.]]
[[Category: Kaczor-Grzeskowiak, M.]]
[[Category: Kopka, M.L.]]
[[Category: Kopka, M L.]]
[[Category: Maris, A.E.]]
[[Category: Maris, A E.]]
[[Category: Sawaya, M.R.]]
[[Category: Sawaya, M R.]]
[[Category: Schroder, I.]]
[[Category: Schroder, I.]]
[[Category: SO4]]
[[Category: SO4]]
Line 28: Line 28:
[[Category: two-component response regulator]]
[[Category: two-component response regulator]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:09:26 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:39 2008''

Revision as of 14:21, 21 February 2008

File:1je8.gif


1je8, resolution 2.12Å

Drag the structure with the mouse to rotate

Two-Component response regulator NarL/DNA Complex: DNA Bending Found in a High Affinity Site

OverviewOverview

Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component response regulators can bind DNA. DNA recognition is accompanied by the formation of a new dimerization interface, which could occur only in the full-length protein via a large intramolecular domain rearrangement. The DNA is recognized by the concerted effects of solvation, van der Waals forces and inherent DNA deformability, rather than determined primarily by major groove hydrogen bonding. These subtle forces permit a small DNA-binding domain to perturb the DNA helix, leading to major DNA curvature and a transition from B- to A-form DNA at the binding site, where valine on the recognition helix interacts unexpectedly with the polar major groove floor.

About this StructureAbout this Structure

1JE8 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Dimerization allows DNA target site recognition by the NarL response regulator., Maris AE, Sawaya MR, Kaczor-Grzeskowiak M, Jarvis MR, Bearson SM, Kopka ML, Schroder I, Gunsalus RP, Dickerson RE, Nat Struct Biol. 2002 Oct;9(10):771-8. PMID:12352954

Page seeded by OCA on Thu Feb 21 13:21:39 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA