2y1b

Crystal structure of the E. coli outer membrane lipoprotein RcsF

spinqualitylabelsall models 2y1b, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y1b is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: I3C, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RCSF_ECOLI Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division. Publication Abstract from PubMed The bacterial Rcs phosphorelay is a stress-induced defense mechanism that controls the expression of numerous genes, including those for capsular polysaccharides, motility, and virulence factors. It is a complex multicomponent system that includes the histidine kinase (RcsC) and the response regulator (RcsB) and also auxiliary proteins such as RcsF. RcsF is an outer membrane lipoprotein that transmits signals from the cell surface to RcsC. The physiological signals that activate RcsF and how RcsF interacts with RcsC remain unknown. Here, we report the three-dimensional structure of RcsF. The fold of the protein is characterized by the presence of a central 4-stranded beta sheet, which is conserved in several other proteins, including the copper-binding domain of the amyloid precursor protein. RcsF, which contains four conserved cysteine residues, presents two nonconsecutive disulfides between Cys(74) and Cys(118) and between Cys(109) and Cys(124), respectively. These two disulfides are not functionally equivalent; the Cys(109)-Cys(124) disulfide is particularly important for the assembly of an active RcsF. Moreover, we show that formation of the nonconsecutive disulfides of RcsF depends on the periplasmic disulfide isomerase DsbC. We trapped RcsF in a mixed disulfide complex with DsbC, and we show that deletion of dsbC prevents the activation of the Rcs phosphorelay by signals that function through RcsF. The three-dimensional structure of RcsF provides the structural basis to understand how this protein triggers the Rcs signaling cascade. Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC.,Leverrier P, Declercq JP, Denoncin K, Vertommen D, Hiniker A, Cho SH, Collet JF J Biol Chem. 2011 May 13;286(19):16734-42. Epub 2011 Mar 16. PMID:21454485 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA