2L0L
DsbB2 peptide structure in 70% TFE
Summary for 2L0L
| Entry DOI | 10.2210/pdb2l0l/pdb |
| Related | 2K73 2ZUQ |
| Descriptor | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I (1 entity in total) |
| Functional Keywords | dsbb, membrane protein, organic solvent, folding |
| Biological source | Escherichia coli BW2952 |
| Cellular location | Cell inner membrane; Multi-pass membrane protein (By similarity): C4ZTM6 |
| Total number of polymer chains | 1 |
| Total formula weight | 2832.49 |
| Authors | |
| Primary citation | Hwang, S.,Hilty, C. Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy. Proteins, 79:1365-1375, 2011 Cited by PubMed Abstract: The two-stage model for membrane protein folding postulates that individual helices form first and are subsequently packed against each other. To probe the two-stage model, the structures of peptides representing individual transmembrane helices of the disulfide bond forming protein B have been studied in trifluoroethanol solution as well as in detergent micelles using nuclear magnetic resonance (NMR) and circular dichroism spectroscopy. In TFE solution, peptides showed well-defined α-helical structures. Peptide structures in TFE were compared to the structures of full-length protein obtained by X-ray crystallography and NMR. The extent of α-helical secondary structure coincided well, lending support for the two-stage model for membrane protein folding. However, the conformation of some amino acid side chains differs between the structures of peptide and full-length protein. In micellar solution, the peptides also adopted a helical structure, albeit of reduced definition. Using measurements of paramagnetic relaxation enhancement, peptides were confirmed to be embedded in micelles. These observations may indicate that in the native protein, tertiary interactions additionally stabilize the secondary structure of the individual transmembrane helices. PubMed: 21337621DOI: 10.1002/prot.22877 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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