1fzp
From Proteopedia
(New page: 200px<br /><applet load="1fzp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fzp, resolution 2.95Å" /> '''CRYSTAL STRUCTURES O...) |
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| - | [[Image:1fzp.gif|left|200px]]<br /><applet load="1fzp" size=" | + | [[Image:1fzp.gif|left|200px]]<br /><applet load="1fzp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fzp, resolution 2.95Å" /> | caption="1fzp, resolution 2.95Å" /> | ||
'''CRYSTAL STRUCTURES OF SARA: A PLEIOTROPIC REGULATOR OF VIRULENCE GENES IN S. AUREUS'''<br /> | '''CRYSTAL STRUCTURES OF SARA: A PLEIOTROPIC REGULATOR OF VIRULENCE GENES IN S. AUREUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Staphylococcus aureus is a major human pathogen, the potency of which can | + | Staphylococcus aureus is a major human pathogen, the potency of which can be attributed to the regulated expression of an impressive array of virulence determinants. A key pleiotropic transcriptional regulator of these virulence factors is SarA, which is encoded by the sar (staphylococcal accessory regulator) locus. SarA was characterized initially as an activator of a second virulence regulatory locus, agr, through its interaction with a series of heptad repeats (AGTTAAG) within the agr promoter. Subsequent DNA-binding studies have revealed that SarA binds readily to multiple AT-rich sequences of variable lengths. Here we describe the crystal structure of SarA and a SarA-DNA complex at resolutions of 2.50 A and 2.95 A, respectively. SarA has a fold consisting of a four-helix core region and 'inducible regions' comprising a beta-hairpin and a carboxy-terminal loop. On binding DNA, the inducible regions undergo marked conformational changes, becoming part of extended and distorted alpha-helices, which encase the DNA. SarA recognizes an AT-rich site in which the DNA is highly overwound and adopts a D-DNA-like conformation by indirect readout. These structures thus provide insight into SarA-mediated transcription regulation. |
==About this Structure== | ==About this Structure== | ||
| - | 1FZP 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:// | + | 1FZP 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=1FZP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Brennan, R | + | [[Category: Brennan, R G.]] |
[[Category: Hurlburt, B.]] | [[Category: Hurlburt, B.]] | ||
| - | [[Category: Schumacher, M | + | [[Category: Schumacher, M A.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: coil to helix]] | [[Category: coil to helix]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:24 2008'' |
Revision as of 10:44, 21 February 2008
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CRYSTAL STRUCTURES OF SARA: A PLEIOTROPIC REGULATOR OF VIRULENCE GENES IN S. AUREUS
Overview
Staphylococcus aureus is a major human pathogen, the potency of which can be attributed to the regulated expression of an impressive array of virulence determinants. A key pleiotropic transcriptional regulator of these virulence factors is SarA, which is encoded by the sar (staphylococcal accessory regulator) locus. SarA was characterized initially as an activator of a second virulence regulatory locus, agr, through its interaction with a series of heptad repeats (AGTTAAG) within the agr promoter. Subsequent DNA-binding studies have revealed that SarA binds readily to multiple AT-rich sequences of variable lengths. Here we describe the crystal structure of SarA and a SarA-DNA complex at resolutions of 2.50 A and 2.95 A, respectively. SarA has a fold consisting of a four-helix core region and 'inducible regions' comprising a beta-hairpin and a carboxy-terminal loop. On binding DNA, the inducible regions undergo marked conformational changes, becoming part of extended and distorted alpha-helices, which encase the DNA. SarA recognizes an AT-rich site in which the DNA is highly overwound and adopts a D-DNA-like conformation by indirect readout. These structures thus provide insight into SarA-mediated transcription regulation.
About this Structure
1FZP is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus., Schumacher MA, Hurlburt BK, Brennan RG, Nature. 2001 Jan 11;409(6817):215-9. PMID:11196648
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