1OR7

Crystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseA

Summary for 1OR7

• Entry DOI: 10.2210/pdb1or7/pdb
• Descriptor: RNA polymerase sigma-E factor, Sigma-E factor negative regulatory protein (3 entities in total)
• Functional Keywords: regulation, dna-binding, transmembrane, transcription
• Biological source: Escherichia coli; More
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P0AFX7
• Total number of polymer chains: 4
• Total formula weight: 64825.41

Authors

Campbell, E.A.,Tupy, J.L.,Gruber, T.M.,Wang, S.,Sharp, M.M.,Gross, C.A.,Darst, S.A. (deposition date: 2003-03-12, release date: 2003-04-15, Last modification date: 2024-02-14)

Primary citation

Campbell, E.A.,Tupy, J.L.,Gruber, T.M.,Wang, S.,Sharp, M.M.,Gross, C.A.,Darst, S.A.
Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA.
Mol.Cell, 11:1067-1078, 2003

PubMed Abstract: The sigma factors are the key regulators of bacterial transcription. ECF (extracytoplasmic function) sigma's are the largest and most divergent group of sigma(70) family members. ECF sigma's are normally sequestered in an inactive complex by their specific anti-sigma factor, which often spans the inner membrane. Here, we determined the 2 A resolution crystal structure of the Escherichia coli ECF sigma factor sigma(E) in an inhibitory complex with the cytoplasmic domain of its anti-sigma, RseA. Despite extensive sequence variability, the two major domains of sigma(E) are virtually identical in structure to the corresponding domains of other sigma(70) family members. In combination with a model of the sigma(E) holoenzyme and biochemical data, the structure reveals that RseA functions by sterically occluding the two primary binding determinants on sigma(E) for core RNA polymerase.

PubMed: 12718891
DOI: 10.1016/S1097-2765(03)00148-5

Experimental method

X-RAY DIFFRACTION (2 Å)