2Q1Z

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

Summary for 2Q1Z

• Entry DOI: 10.2210/pdb2q1z/pdb
• Related: 2Z2S
• Descriptor: RpoE, ECF SigE, Anti-Sigma factor ChrR, transcriptional activator ChrR, ZINC ION (3 entities in total)
• Functional Keywords: ecf sigma factor, anti-sigma factor, cupin fold, zinc binding transcription factor, transcription
• Biological source: Rhodobacter sphaeroides; More
• Total number of polymer chains: 4
• Total formula weight: 83692.06

Authors

Campbell, E.A.,Darst, S.A. (deposition date: 2007-05-25, release date: 2007-09-18, Last modification date: 2024-02-21)

Primary citation

Campbell, E.A.,Greenwell, R.,Anthony, J.R.,Wang, S.,Lim, L.,Das, K.,Sofia, H.J.,Donohue, T.J.,Darst, S.A.
A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria.
Mol.Cell, 27:793-805, 2007

PubMed Abstract: 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.

PubMed: 17803943
DOI: 10.1016/j.molcel.2007.07.009

Experimental method

X-RAY DIFFRACTION (2.4 Å)