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1zes

From Proteopedia

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[[Image:1zes.gif|left|200px]]
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{{STRUCTURE_1zes| PDB=1zes | SCENE= }}
{{STRUCTURE_1zes| PDB=1zes | SCENE= }}
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'''BeF3- activated PhoB receiver domain'''
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===BeF3- activated PhoB receiver domain===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16154092 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16154092}}
==About this Structure==
==About this Structure==
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[[Category: Response regulator]]
[[Category: Response regulator]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:32:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:19:04 2008''

Revision as of 11:19, 27 July 2008

Image:1zes.png

Template:STRUCTURE 1zes

BeF3- activated PhoB receiver domain

Template:ABSTRACT PUBMED 16154092

About this Structure

1ZES is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

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:16154092

Page seeded by OCA on Sun Jul 27 14:19:04 2008

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