2LTQ
High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data
Summary for 2LTQ
| Entry DOI | 10.2210/pdb2ltq/pdb |
| Related | 2LEG 2ZUQ |
| NMR Information | BMRB: 18493 |
| Descriptor | Disulfide bond formation protein B, Fab fragment light chain, Fab fragment heavy chain, ... (4 entities in total) |
| Functional Keywords | membrane protein, oxidoreductase, disulfide bond, redox-active center, cell inner membrane, cell membrane, chaperone, electron transport, membrane, transmembrane, transport |
| Biological source | Escherichia coli (strain K12) More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P0A6M2 |
| Total number of polymer chains | 6 |
| Total formula weight | 141729.91 |
| Authors | Tang, M.,Sperling, L.J.,Schwieters, C.D.,Nesbitt, A.E.,Gennis, R.B.,Rienstra, C.M. (deposition date: 2012-05-30, release date: 2013-02-27, Last modification date: 2024-11-27) |
| Primary citation | Tang, M.,Nesbitt, A.E.,Sperling, L.J.,Berthold, D.A.,Schwieters, C.D.,Gennis, R.B.,Rienstra, C.M. Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer. J.Mol.Biol., 425:1670-1682, 2013 Cited by PubMed Abstract: 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. PubMed: 23416557DOI: 10.1016/j.jmb.2013.02.009 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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