Participation of the BC Loop in the Correct Folding of Bacteriorhodopsin as Revealed by Solid-state NMR
| العنوان: | Participation of the BC Loop in the Correct Folding of Bacteriorhodopsin as Revealed by Solid-state NMR |
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| المؤلفون: | Izuru Kawamura, Satoru Tuzi, Akira Naito, Satoru Yamaguchi, Junko Tanabe, Masato Ohmine |
| المصدر: | Photochemistry and Photobiology. 85:624-630 |
| بيانات النشر: | Wiley, 2009. |
| سنة النشر: | 2009 |
| مصطلحات موضوعية: | Halobacterium salinarum, Models, Molecular, Protein Folding, biology, Molecular Sequence Data, Retinal, Bacteriorhodopsin, General Medicine, Carbon-13 NMR, Biochemistry, Protein Structure, Tertiary, NMR spectra database, chemistry.chemical_compound, Crystallography, Protein structure, chemistry, Solid-state nuclear magnetic resonance, Bacteriorhodopsins, biology.protein, Amino Acid Sequence, Physical and Theoretical Chemistry, Nuclear Magnetic Resonance, Biomolecular |
| الوصف: | Structural changes in bacteriorhodopsin (bR) in two different processes of retinal reconstitutions were investigated by observing the (13)C and (15)N solid-state NMR spectra of [1-(13)C]Val- and [(15)N]Pro-labeled bR. We found that NMR signals of the BC loop were sensitive to changes in protein structure and dynamics, from wild-type (WT) bR to bacterio-opsin (bO), regenerated bR and E1001 bR. Regenerated bR was prepared following the addition of retinal into bO obtained from photobleached WT-bR. E1001 bR was cultured from a retinal-deficient strain termed E1001 following the addition of retinal to growing cells. (15)N NMR signal at Pro70 in the BC loop in WT-bR was observed at 122.4 p.p.m., whereas signals were not apparent or partly suppressed in bO and regenerated bR, respectively. Similarly, the (13)C NMR signal at Val69 in the BC loop at 172.0 p.p.m. that was observed in WT-bR was significantly decreased in both regenerated bR and bO. These results suggest that the dynamic structure of the BC loop in bO was substantially altered following the removal of retinal. As a consequence, the correct protein structure failed to be recovered via the regenerating process of retinal to bO. On the other hand, (13)C and (15)N NMR signals at the BC loop in E1001 bR appeared at positions identical to those of WT-bR. The results of the current study indicate that the BC loop may not always fold correctly in the regenerated bR, which leads to different properties in the regenerated bR compared to that of WT-bR. |
| تدمد: | 1751-1097 0031-8655 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49dba8c6913efa09591cbd30d51c65af https://doi.org/10.1111/j.1751-1097.2009.00536.x |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....49dba8c6913efa09591cbd30d51c65af |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17511097 00318655 |
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