| FTIR study of the L intermediate of Anabaena sensory rhodopsin: structural changes in the cytoplasmic region. | |
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MedLine Citation:
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PMID: 18759456 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Anabaena sensory rhodopsin (ASR) is an archaeal-type rhodopsin found in eubacteria. The gene encoding ASR forms a single operon with ASRT (ASR transducer) that is a 14 kDa soluble protein, suggesting that ASR functions as a photochromic sensor by activating the soluble transducer. One of the characteristics of ASR is that the formation of the M intermediate accompanies a proton transfer from the Schiff base to Asp217 in the cytoplasmic side [Shi, L., Yoon, S. R., Bezerra, A. G., Jr., Jung, K. H., and Brown, L. S. (2006) J. Mol. Biol. 358, 686-700], in remarkable contrast to other archaeal-type rhodopsins such as a light-driven proton-pump, bacteriorhodopsin (BR). In this study, we applied low-temperature Fourier transform infrared (FTIR) spectroscopy to the all- trans form of ASR at 170 K, and compared the structural changes in the L intermediate with those of BR. The ASR L minus ASR difference spectra were essentially similar to those for BR, suggesting common structures for the L state in ASR and BR. On the other hand, unique CO stretching bands of a protonated carboxylic acid were observed at 1722 (+) and 1703 (-) cm (-1) at pH 5 and 7, and assigned to Glu36 by use of mutants. Glu36 is located at the cytoplasmic side, and the distance from the Schiff base is about 20 A. This result shows the structural changes at the cytoplasmic surface in ASR L. pH-dependent frequency change was also observed for a water stretching vibration, suggesting that the water molecule is involved in a hydrogen-bonding network with Glu36 and Asp217. Unique hydrogen-bonding network in the cytoplasmic domain of ASR will be discussed. |
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Authors:
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Akira Kawanabe; Yuji Furutani; Sa Ryong Yoon; Kwang-Hwan Jung; Hideki Kandori |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't Date: 2008-08-30 |
Journal Detail:
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Title: Biochemistry Volume: 47 ISSN: 1520-4995 ISO Abbreviation: Biochemistry Publication Date: 2008 Sep |
Date Detail:
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Created Date: 2008-09-16 Completed Date: 2008-10-03 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 10033-40 Citation Subset: IM |
Affiliation:
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Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya, 466-8555, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Substitution
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genetics Anabaena / chemistry*, genetics Bacterial Proteins / chemistry*, genetics Cytoplasm / chemistry*, genetics Molecular Conformation Sensory Rhodopsins / chemistry*, genetics Sequence Deletion Spectroscopy, Fourier Transform Infrared / methods |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Sensory Rhodopsins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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