1gxp
From Proteopedia
(New page: 200px<br /><applet load="1gxp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gxp, resolution 2.5Å" /> '''PHOB EFFECTOR DOMAIN ...) |
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| - | [[Image:1gxp.gif|left|200px]]<br /><applet load="1gxp" size=" | + | [[Image:1gxp.gif|left|200px]]<br /><applet load="1gxp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gxp, resolution 2.5Å" /> | caption="1gxp, resolution 2.5Å" /> | ||
'''PHOB EFFECTOR DOMAIN IN COMPLEX WITH PHO BOX DNA.'''<br /> | '''PHOB EFFECTOR DOMAIN IN COMPLEX WITH PHO BOX DNA.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PhoB is a signal transduction response regulator that activates nearly 40 | + | PhoB is a signal transduction response regulator that activates nearly 40 genes in phosphate depletion conditions in E. coli and closely related bacteria. The structure of the PhoB effector domain in complex with its target DNA sequence, or pho box, reveals a novel tandem arrangement in which several monomers bind head to tail to successive 11-base pair direct-repeat sequences, coating one face of a smoothly bent double helix. The protein has a winged helix fold in which the DNA recognition elements comprise helix alpha 3, penetrating the major groove, and a beta hairpin wing interacting with a compressed minor groove via Arg219, tightly sandwiched between the DNA sugar backbones. The transactivation loops protrude laterally in an appropriate orientation to interact with the RNA polymerase sigma(70) subunit, which triggers transcription initiation. |
==About this Structure== | ==About this Structure== | ||
| - | 1GXP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1GXP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1GXP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Blanco, A | + | [[Category: Blanco, A G.]] |
[[Category: Coll, M.]] | [[Category: Coll, M.]] | ||
| - | [[Category: Gomis-Ruth, F | + | [[Category: Gomis-Ruth, F X.]] |
[[Category: Sola, M.]] | [[Category: Sola, M.]] | ||
[[Category: activator]] | [[Category: activator]] | ||
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[[Category: two-component signal transduction]] | [[Category: two-component signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:07 2008'' |
Revision as of 10:55, 21 February 2008
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PHOB EFFECTOR DOMAIN IN COMPLEX WITH PHO BOX DNA.
Overview
PhoB is a signal transduction response regulator that activates nearly 40 genes in phosphate depletion conditions in E. coli and closely related bacteria. The structure of the PhoB effector domain in complex with its target DNA sequence, or pho box, reveals a novel tandem arrangement in which several monomers bind head to tail to successive 11-base pair direct-repeat sequences, coating one face of a smoothly bent double helix. The protein has a winged helix fold in which the DNA recognition elements comprise helix alpha 3, penetrating the major groove, and a beta hairpin wing interacting with a compressed minor groove via Arg219, tightly sandwiched between the DNA sugar backbones. The transactivation loops protrude laterally in an appropriate orientation to interact with the RNA polymerase sigma(70) subunit, which triggers transcription initiation.
About this Structure
1GXP is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator., Blanco AG, Sola M, Gomis-Ruth FX, Coll M, Structure. 2002 May;10(5):701-13. PMID:12015152
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