2oug: Difference between revisions
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[[Image:2oug.gif|left|200px]] | [[Image:2oug.gif|left|200px]] | ||
'''Crystal structure of the RfaH transcription factor at 2.1A resolution''' | {{Structure | ||
|PDB= 2oug |SIZE=350|CAPTION= <scene name='initialview01'>2oug</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= rfaH, hlyT, sfrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal structure of the RfaH transcription factor at 2.1A resolution''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OUG is a [ | 2OUG 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=2OUG OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for converting a general transcription factor into an operon-specific virulence regulator., Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I, Mol Cell. 2007 Apr 13;26(1):117-29. PMID:[http:// | Structural basis for converting a general transcription factor into an operon-specific virulence regulator., Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I, Mol Cell. 2007 Apr 13;26(1):117-29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17434131 17434131] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: virulence]] | [[Category: virulence]] | ||
''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 18:04:38 2008'' | ||
Revision as of 19:04, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Gene: | rfaH, hlyT, sfrB (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the RfaH transcription factor at 2.1A resolution
OverviewOverview
RfaH, a paralog of the general transcription factor NusG, is recruited to elongating RNA polymerase at specific regulatory sites. The X-ray structure of Escherichia coli RfaH reported here reveals two domains. The N-terminal domain displays high similarity to that of NusG. In contrast, the alpha-helical coiled-coil C domain, while retaining sequence similarity, is strikingly different from the beta barrel of NusG. To our knowledge, such an all-beta to all-alpha transition of the entire domain is the most extreme example of protein fold evolution known to date. Both N domains possess a vast hydrophobic cavity that is buried by the C domain in RfaH but is exposed in NusG. We propose that this cavity constitutes the RNA polymerase-binding site, which becomes unmasked in RfaH only upon sequence-specific binding to the nontemplate DNA strand that triggers domain dissociation. Finally, we argue that RfaH binds to the beta' subunit coiled coil, the major target site for the initiation sigma factors.
About this StructureAbout this Structure
2OUG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for converting a general transcription factor into an operon-specific virulence regulator., Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I, Mol Cell. 2007 Apr 13;26(1):117-29. PMID:17434131
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