1R2N
NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin
Summary for 1R2N
| Entry DOI | 10.2210/pdb1r2n/pdb |
| Related | 1BRR 1c3w 1qhj |
| Descriptor | Bacteriorhodopsin, RETINAL (3 entities in total) |
| Functional Keywords | proton pump, membrane protein, retinal protein, photoreceptor, haloarchaea, proton transport |
| Biological source | Halobacterium salinarium (archaea) |
| Cellular location | Cell membrane; Multi-pass membrane protein: P02945 |
| Total number of polymer chains | 1 |
| Total formula weight | 27213.94 |
| Authors | Patzelt, H.,Simon, B.,terLaak, A.,Kessler, B.,Kuhne, R.,Schmieder, P.,Oesterhaelt, D.,Oschkinat, H. (deposition date: 2003-09-29, release date: 2003-10-28, Last modification date: 2022-03-02) |
| Primary citation | Patzelt, H.,Simon, B.,terLaak, A.,Kessler, B.,Kuhne, R.,Schmieder, P.,Oesterhaelt, D.,Oschkinat, H. The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy Proc.Natl.Acad.Sci.USA, 99:9765-9770, 2002 Cited by PubMed Abstract: The two forms of bacteriorhodopsin present in the dark-adapted state, containing either all-trans or 13-cis,15-syn retinal, were examined by using solution state NMR, and their structures were determined. Comparison of the all-trans and the 13-cis,15-syn forms shows a shift in position of about 0.25 A within the pocket of the protein. Comparing this to the 13-cis,15-anti chromophore of the catalytic cycle M-intermediate structure, the 13-cis,15-syn form demonstrates a less pronounced up-tilt of the retinal C12[bond]C14 region, while leaving W182 and T178 essentially unchanged. The N[bond]H dipole of the Schiff base orients toward the extracellular side in both forms, however, it reorients toward the intracellular side in the 13-cis,15-anti configuration to form the catalytic M-intermediate. Thus, the change of the N[bond]H dipole is considered primarily responsible for energy storage, conformation changes of the protein, and the deprotonation of the Schiff base. The structural similarity of the all-trans and 13-cis,15-syn forms is taken as strong evidence for the ion dipole dragging model by which proton (hydroxide ion) translocation follows the change of the dipole. PubMed: 12119389DOI: 10.1073/pnas.132253899 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
