2p4b: Difference between revisions

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==Overview==

The bacterial envelope stress response senses stress signals in the, extracytoplasmic compartment, and activates sigma(E)-dependent, transcription by degrading its antisigma factor RseA. RseB, a binding, partner of RseA, plays a pivotal role in regulating this response, but its, molecular mechanism is not understood. We therefore determined the crystal, structure of Escherichia coli RseB at a resolution of 2.4 A. RseB is, composed of two domains linked by a flexible linker and forms a loosely, packed dimer with two grooves on each side. This structural feature is, confirmed by small-angle scattering in solution. Analysis of the binding, of various RseA mutants to RseB allowed us to identify the major, RseB-binding motif in RseA. These data, coupled with analysis of, small-angle scattering of the RseA/RseB complex in solution, leads us to, propose that two RseAs bind to the grooves of the dimeric RseB by, conserved residues. The implications for modulating proteolytic cleavage, of RseA are discussed.

The bacterial envelope stress response senses stress signals in the extracytoplasmic compartment, and activates sigma(E)-dependent transcription by degrading its antisigma factor RseA. RseB, a binding partner of RseA, plays a pivotal role in regulating this response, but its molecular mechanism is not understood. We therefore determined the crystal structure of Escherichia coli RseB at a resolution of 2.4 A. RseB is composed of two domains linked by a flexible linker and forms a loosely packed dimer with two grooves on each side. This structural feature is confirmed by small-angle scattering in solution. Analysis of the binding of various RseA mutants to RseB allowed us to identify the major RseB-binding motif in RseA. These data, coupled with analysis of small-angle scattering of the RseA/RseB complex in solution, leads us to propose that two RseAs bind to the grooves of the dimeric RseB by conserved residues. The implications for modulating proteolytic cleavage of RseA are discussed.

==About this Structure==

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[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Kim, D.Y.]]

[[Category: Kim, D Y.]]

[[Category: Kim, K.K.]]

[[Category: Kim, K K.]]

[[Category: BOG]]

[[Category: open and closed form]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The bacterial envelope stress response senses stress signals in the, extracytoplasmic compartment, and activates sigma(E)-dependent, transcription by degrading its antisigma factor RseA. RseB, a binding, partner of RseA, plays a pivotal role in regulating this response, but its, molecular mechanism is not understood. We therefore determined the crystal, structure of Escherichia coli RseB at a resolution of 2.4 A. RseB is, composed of two domains linked by a flexible linker and forms a loosely, packed dimer with two grooves on each side. This structural feature is, confirmed by small-angle scattering in solution. Analysis of the binding, of various RseA mutants to RseB allowed us to identify the major, RseB-binding motif in RseA. These data, coupled with analysis of, small-angle scattering of the RseA/RseB complex in solution, leads us to, propose that two RseAs bind to the grooves of the dimeric RseB by, conserved residues. The implications for modulating proteolytic cleavage, of RseA are discussed.
+The bacterial envelope stress response senses stress signals in the extracytoplasmic compartment, and activates sigma(E)-dependent transcription by degrading its antisigma factor RseA. RseB, a binding partner of RseA, plays a pivotal role in regulating this response, but its molecular mechanism is not understood. We therefore determined the crystal structure of Escherichia coli RseB at a resolution of 2.4 A. RseB is composed of two domains linked by a flexible linker and forms a loosely packed dimer with two grooves on each side. This structural feature is confirmed by small-angle scattering in solution. Analysis of the binding of various RseA mutants to RseB allowed us to identify the major RseB-binding motif in RseA. These data, coupled with analysis of small-angle scattering of the RseA/RseB complex in solution, leads us to propose that two RseAs bind to the grooves of the dimeric RseB by conserved residues. The implications for modulating proteolytic cleavage of RseA are discussed.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Kim, D.Y.]]
+[[Category: Kim, D Y.]]
-[[Category: Kim, K.K.]]
+[[Category: Kim, K K.]]
 [[Category: BOG]]
 [[Category: open and closed form]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:59:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:39 2008''