2z2s
From Proteopedia
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- | [[Image:2z2s.jpg|left|200px]] | + | [[Image:2z2s.jpg|left|200px]] |
- | + | ||
- | '''Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR''' | + | {{Structure |
+ | |PDB= 2z2s |SIZE=350|CAPTION= <scene name='initialview01'>2z2s</scene>, resolution 2.7Å | ||
+ | |SITE= <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> | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= rpoE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]), chrR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2Z2S is a [ | + | 2Z2S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2S OCA]. |
==Reference== | ==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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/17803943 17803943] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
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[[Category: zinc binding transcription factor]] | [[Category: zinc binding transcription factor]] | ||
- | ''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 18:51:31 2008'' |
Revision as of 16:51, 20 March 2008
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, resolution 2.7Å | |||||||
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Sites: | , , , , and | ||||||
Ligands: | and | ||||||
Gene: | rpoE (Rhodobacter sphaeroides), chrR (Rhodobacter sphaeroides) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
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