1or7
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(New page: 200px<br /><applet load="1or7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1or7, resolution 2.00Å" /> '''Crystal Structure of...)
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Revision as of 21:00, 20 November 2007
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Crystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseA
Overview
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.
About this Structure
1OR7 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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