1gxq
From Proteopedia
(New page: 200px<br /><applet load="1gxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gxq, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1gxq.gif|left|200px]]<br /><applet load="1gxq" size=" | + | [[Image:1gxq.gif|left|200px]]<br /><applet load="1gxq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gxq, resolution 2.00Å" /> | caption="1gxq, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF THE PHOB EFFECTOR DOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE PHOB EFFECTOR DOMAIN'''<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== | ||
| - | 1GXQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1GXQ is a [http://en.wikipedia.org/wiki/Single_protein 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=1GXQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[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 12:55:08 2008'' |
Revision as of 10:55, 21 February 2008
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CRYSTAL STRUCTURE OF THE PHOB EFFECTOR DOMAIN
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
1GXQ is a Single protein structure of sequence 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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