2frh
From Proteopedia
(New page: 200px<br /><applet load="2frh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2frh, resolution 2.50Å" /> '''Crystal Structure of...) |
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| - | [[Image:2frh.jpg|left|200px]]<br /><applet load="2frh" size=" | + | [[Image:2frh.jpg|left|200px]]<br /><applet load="2frh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2frh, resolution 2.50Å" /> | caption="2frh, resolution 2.50Å" /> | ||
'''Crystal Structure of Sara, A Transcription Regulator From Staphylococcus Aureus'''<br /> | '''Crystal Structure of Sara, A Transcription Regulator From Staphylococcus Aureus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The sarA locus in Staphylococcus aureus controls the expression of many | + | The sarA locus in Staphylococcus aureus controls the expression of many virulence genes. The sarA regulatory molecule, SarA, is a 14.7-kDa protein (124 residues) that binds to the promoter region of target genes. Here we report the 2.6 A-resolution x-ray crystal structure of the dimeric winged helix SarA protein, which differs from the published SarA structure dramatically. In the crystal packing, multiple dimers of SarA form a scaffold, possibly via divalent cations. Mutations of individual residues within the DNA-binding helix-turn-helix and the winged region as well as within the metal-binding pocket implicate basic residues R84 and R90 within the winged region to be critical in DNA binding, whereas acidic residues D88 and E89 (wing), D8 and E11 (metal-binding pocket), and cysteine 9 are essential for SarA function. These data suggest that the winged region of the winged helix protein participates in DNA binding and activation, whereas the putative divalent cation binding pocket is only involved in gene function. |
==About this Structure== | ==About this Structure== | ||
| - | 2FRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FRH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Cheung, A | + | [[Category: Cheung, A L.]] |
[[Category: Ingavale, S.]] | [[Category: Ingavale, S.]] | ||
[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
| - | [[Category: Manna, A | + | [[Category: Manna, A C.]] |
[[Category: Zhang, G.]] | [[Category: Zhang, G.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: winged-helix protein]] | [[Category: winged-helix protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:30 2008'' |
Revision as of 15:24, 21 February 2008
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Crystal Structure of Sara, A Transcription Regulator From Staphylococcus Aureus
Overview
The sarA locus in Staphylococcus aureus controls the expression of many virulence genes. The sarA regulatory molecule, SarA, is a 14.7-kDa protein (124 residues) that binds to the promoter region of target genes. Here we report the 2.6 A-resolution x-ray crystal structure of the dimeric winged helix SarA protein, which differs from the published SarA structure dramatically. In the crystal packing, multiple dimers of SarA form a scaffold, possibly via divalent cations. Mutations of individual residues within the DNA-binding helix-turn-helix and the winged region as well as within the metal-binding pocket implicate basic residues R84 and R90 within the winged region to be critical in DNA binding, whereas acidic residues D88 and E89 (wing), D8 and E11 (metal-binding pocket), and cysteine 9 are essential for SarA function. These data suggest that the winged region of the winged helix protein participates in DNA binding and activation, whereas the putative divalent cation binding pocket is only involved in gene function.
About this Structure
2FRH is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural and function analyses of the global regulatory protein SarA from Staphylococcus aureus., Liu Y, Manna AC, Pan CH, Kriksunov IA, Thiel DJ, Cheung AL, Zhang G, Proc Natl Acad Sci U S A. 2006 Feb 14;103(7):2392-7. Epub 2006 Feb 2. PMID:16455801
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