1xhf
From Proteopedia
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{{STRUCTURE_1xhf| PDB=1xhf | SCENE= }} | {{STRUCTURE_1xhf| PDB=1xhf | SCENE= }} | ||
===Crystal structure of the bef3-activated receiver domain of redox response regulator arca=== | ===Crystal structure of the bef3-activated receiver domain of redox response regulator arca=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1xhf]] is a 2 chain structure of [[Response regulator]] with 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=1XHF OCA]. | |
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| + | ==See Also== | ||
| + | *[[Response regulator|Response regulator]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015876365</ref><ref group="xtra">PMID:018557815</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Mack, T R.]] | [[Category: Mack, T R.]] | ||
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[[Category: Doubly wound five-stranded beta/alpha fold]] | [[Category: Doubly wound five-stranded beta/alpha fold]] | ||
[[Category: Gene regulation]] | [[Category: Gene regulation]] | ||
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[[Category: Transcription factor]] | [[Category: Transcription factor]] | ||
[[Category: Two-component system]] | [[Category: Two-component system]] | ||
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Revision as of 09:47, 25 July 2012
Contents |
Crystal structure of the bef3-activated receiver domain of redox response regulator arca
Template:ABSTRACT PUBMED 15876365
About this Structure
1xhf is a 2 chain structure of Response regulator with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Toro-Roman A, Mack TR, Stock AM. Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face. J Mol Biol. 2005 May 27;349(1):11-26. Epub 2005 Apr 7. PMID:15876365 doi:10.1016/j.jmb.2005.03.059
- Thomas SA, Brewster JA, Bourret RB. Two variable active site residues modulate response regulator phosphoryl group stability. Mol Microbiol. 2008 Jul;69(2):453-65. PMID:18557815 doi:10.1111/j.1365-2958.2008.06296.x
