2ltq

High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data

spinqualitylabelsall models 2ltq Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ltq is a 6 chain structure with sequence from Escherichia coli K-12 and Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solid-state NMR, 10 models Ligands: UQ8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The integral membrane protein DsbB in Escherichia coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. We have developed a high-resolution structural model by combining experimental X-ray and solid-state NMR with molecular dynamics (MD) simulations. We embedded the high-resolution DsbB structure, derived from the joint calculation with X-ray reflections and solid-state NMR restraints, into the lipid bilayer and performed MD simulations to provide a mechanistic view of DsbB function in the membrane. Further, we revealed the membrane topology of DsbB by selective proton spin diffusion experiments, which directly probe the correlations of DsbB with water and lipid acyl chains. NMR data also support the model of a flexible periplasmic loop and an interhelical hydrogen bond between Glu26 and Tyr153. Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer.,Tang M, Nesbitt AE, Sperling LJ, Berthold DA, Schwieters CD, Gennis RB, Rienstra CM J Mol Biol. 2013 Feb 14. pii: S0022-2836(13)00095-8. doi:, 10.1016/j.jmb.2013.02.009. PMID:23416557 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thiol:disulfide interchange protein 3D structures

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