1zes: Difference between revisions
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[[Image:1zes.gif|left|200px]] | [[Image:1zes.gif|left|200px]] | ||
'''BeF3- activated PhoB receiver domain''' | {{Structure | ||
|PDB= 1zes |SIZE=350|CAPTION= <scene name='initialview01'>1zes</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=BEF:BERYLLIUM TRIFLUORIDE ION'>BEF</scene> | |||
|ACTIVITY= | |||
|GENE= phoB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''BeF3- activated PhoB receiver domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZES is a [ | 1ZES is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZES OCA]. | ||
==Reference== | ==Reference== | ||
Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states., Bachhawat P, Swapna GV, Montelione GT, Stock AM, Structure. 2005 Sep;13(9):1353-63. PMID:[http:// | Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states., Bachhawat P, Swapna GV, Montelione GT, Stock AM, Structure. 2005 Sep;13(9):1353-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16154092 16154092] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:34 2008'' | ||
Revision as of 16:34, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | phoB (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BeF3- activated PhoB receiver domain
OverviewOverview
Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiver domain that regulates the activities of a C-terminal DNA binding domain in a phosphorylation-dependent manner. We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. These structures, together with the previously determined structure of the C-terminal domain of PhoB bound to DNA, define the conformation of the active transcription factor and provide a model for the mechanism of activation in the OmpR/PhoB subfamily, the largest group of RRs. In the active state, the receiver domains dimerize with 2-fold rotational symmetry using their alpha4-beta5-alpha5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.
About this StructureAbout this Structure
1ZES is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states., Bachhawat P, Swapna GV, Montelione GT, Stock AM, Structure. 2005 Sep;13(9):1353-63. PMID:16154092
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