2z2s

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{{STRUCTURE_2z2s| PDB=2z2s | SCENE= }}
{{STRUCTURE_2z2s| PDB=2z2s | SCENE= }}
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'''Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR'''
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===Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17803943 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17803943}}
==About this Structure==
==About this Structure==
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[[Category: Zinc]]
[[Category: Zinc]]
[[Category: Zinc binding transcription factor]]
[[Category: Zinc binding transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:52:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:02:09 2008''

Revision as of 02:02, 29 July 2008

Image:2z2s.png

Template:STRUCTURE 2z2s

Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR

Template:ABSTRACT PUBMED 17803943

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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