2P4B
Crystal structure of E.coli RseB
Summary for 2P4B
| Entry DOI | 10.2210/pdb2p4b/pdb |
| Descriptor | Sigma-E factor regulatory protein rseB, octyl beta-D-glucopyranoside (3 entities in total) |
| Functional Keywords | open and closed form, signaling protein |
| Biological source | Escherichia coli K12 |
| Cellular location | Periplasm (Potential): P0AFX9 |
| Total number of polymer chains | 3 |
| Total formula weight | 100278.62 |
| Authors | |
| Primary citation | Kim, D.Y.,Jin, K.S.,Kwon, E.,Ree, M.,Kim, K.K. Crystal structure of RseB and a model of its binding mode to RseA Proc.Natl.Acad.Sci.Usa, 104:8779-8784, 2007 Cited by PubMed Abstract: 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. PubMed: 17496148DOI: 10.1073/pnas.0703117104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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