1or7
Crystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseACrystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseA
Structural highlights
Function[RPOE_ECOLI] Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane.[1] [2] [3] [4] [5] [6] [RSEA_ECOLI] Negative regulator of RpoE. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA.,Campbell EA, Tupy JL, Gruber TM, Wang S, Sharp MM, Gross CA, Darst SA Mol Cell. 2003 Apr;11(4):1067-78. PMID:12718891[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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