2z2s
From Proteopedia
(New page: 200px<br /><applet load="2z2s" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z2s" /> ''''''<br /> ==About this Structure== is a [h...) |
|||
| Line 1: | Line 1: | ||
[[Image:2z2s.jpg|left|200px]]<br /><applet load="2z2s" size="350" color="white" frame="true" align="right" spinBox="true" | [[Image:2z2s.jpg|left|200px]]<br /><applet load="2z2s" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2z2s" /> | + | caption="2z2s, resolution 2.7Å" /> |
| - | ''''''<br /> | + | '''Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR'''<br /> |
| + | |||
| + | ==Overview== | ||
| + | A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is, controlled by the group IV sigma factor sigma(E) and its cognate, anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a, modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma, domain (ASD) binds a Zn(2+) ion, contacts sigma(E), and is sufficient to, inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain, adopts a cupin fold, can coordinate an additional Zn(2+), and is required, for the transcriptional response to singlet oxygen. Structure-based, sequence analyses predict that the ASD defines a common structural fold, among predicted group IV anti-sigmas. These ASDs are fused to diverse, C-terminal domains that are likely involved in responding to specific, environmental signals that control the activity of their cognate sigma, factor. | ||
==About this Structure== | ==About this Structure== | ||
| - | + | 2Z2S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+B+1'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+H+1'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+D+1'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+F+1'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+E+1'>AC5</scene> and <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+G+2'>AC6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2S OCA]. | |
| + | |||
| + | ==Reference== | ||
| + | A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria., Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA, Mol Cell. 2007 Sep 7;27(5):793-805. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17803943 17803943] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| + | [[Category: Rhodobacter sphaeroides]] | ||
| + | [[Category: Campbell, E.A.]] | ||
| + | [[Category: Darst, S.A.]] | ||
| + | [[Category: SO4]] | ||
| + | [[Category: ZN]] | ||
| + | [[Category: activator]] | ||
| + | [[Category: anti-sigma factor]] | ||
| + | [[Category: cupin fold]] | ||
| + | [[Category: dna-binding]] | ||
| + | [[Category: ecf sigma factor]] | ||
| + | [[Category: metal-binding]] | ||
| + | [[Category: transcription]] | ||
| + | [[Category: transcription regulation]] | ||
| + | [[Category: zinc]] | ||
| + | [[Category: zinc binding transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:24:56 2008'' |
Revision as of 15:24, 6 February 2008
|
Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR
Overview
A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is, controlled by the group IV sigma factor sigma(E) and its cognate, anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a, modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma, domain (ASD) binds a Zn(2+) ion, contacts sigma(E), and is sufficient to, inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain, adopts a cupin fold, can coordinate an additional Zn(2+), and is required, for the transcriptional response to singlet oxygen. Structure-based, sequence analyses predict that the ASD defines a common structural fold, among predicted group IV anti-sigmas. These ASDs are fused to diverse, C-terminal domains that are likely involved in responding to specific, environmental signals that control the activity of their cognate sigma, factor.
About this Structure
2Z2S is a Protein complex structure of sequences from Rhodobacter sphaeroides with and as ligands. Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.
Reference
A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria., Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA, Mol Cell. 2007 Sep 7;27(5):793-805. PMID:17803943
Page seeded by OCA on Wed Feb 6 17:24:56 2008
