1je8: Difference between revisions
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|PDB= 1je8 |SIZE=350|CAPTION= <scene name='initialview01'>1je8</scene>, resolution 2.12Å | |PDB= 1je8 |SIZE=350|CAPTION= <scene name='initialview01'>1je8</scene>, resolution 2.12Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1rnl|1RNL]], [[1a04|1A04]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1je8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1je8 OCA], [http://www.ebi.ac.uk/pdbsum/1je8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1je8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Sawaya, M R.]] | [[Category: Sawaya, M R.]] | ||
[[Category: Schroder, I.]] | [[Category: Schroder, I.]] | ||
[[Category: dna bending]] | [[Category: dna bending]] | ||
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
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[[Category: two-component response regulator]] | [[Category: two-component response regulator]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:24 2008'' |
Revision as of 21:32, 30 March 2008
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, resolution 2.12Å | |||||||
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Ligands: | , , , , , | ||||||
Related: | 1RNL, 1A04
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
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