Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria
Light-driven proton pumps are present in many organisms. Here, we present a high-resolution structure of a proteorhodopsin from a permafrost bacterium, Exiguobacterium sibiricum rhodopsin (ESR). Contrary to the proton pumps of known structure, ESR possesses three unique features. First, ESR's p...
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ftpubmed:oai:pubmedcentral.nih.gov:3732926 2023-05-15T17:57:48+02:00 Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria Gushchin, Ivan Chervakov, Pavel Kuzmichev, Pavel Popov, Alexander N. Round, Ekaterina Borshchevskiy, Valentin Ishchenko, Andrii Petrovskaya, Lada Chupin, Vladimir Dolgikh, Dmitry A. Arseniev, Alexander S. Kirpichnikov, Mikhail Gordeliy, Valentin 2013-07-30 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3732926 http://www.ncbi.nlm.nih.gov/pubmed/23872846 https://doi.org/10.1073/pnas.1221629110 en eng National Academy of Sciences http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3732926 http://www.ncbi.nlm.nih.gov/pubmed/23872846 http://dx.doi.org/10.1073/pnas.1221629110 Biological Sciences Text 2013 ftpubmed https://doi.org/10.1073/pnas.1221629110 2014-02-02T01:49:02Z Light-driven proton pumps are present in many organisms. Here, we present a high-resolution structure of a proteorhodopsin from a permafrost bacterium, Exiguobacterium sibiricum rhodopsin (ESR). Contrary to the proton pumps of known structure, ESR possesses three unique features. First, ESR's proton donor is a lysine side chain that is situated very close to the bulk solvent. Second, the α-helical structure in the middle of the helix F is replaced by 310- and π-helix–like elements that are stabilized by the Trp-154 and Asn-224 side chains. This feature is characteristic for the proteorhodopsin family of proteins. Third, the proton release region is connected to the bulk solvent by a chain of water molecules already in the ground state. Despite these peculiarities, the positions of water molecule and amino acid side chains in the immediate Schiff base vicinity are very well conserved. These features make ESR a very unusual proton pump. The presented structure sheds light on the large family of proteorhodopsins, for which structural information was not available previously. Text permafrost PubMed Central (PMC) Proceedings of the National Academy of Sciences 110 31 12631 12636 |
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Biological Sciences Gushchin, Ivan Chervakov, Pavel Kuzmichev, Pavel Popov, Alexander N. Round, Ekaterina Borshchevskiy, Valentin Ishchenko, Andrii Petrovskaya, Lada Chupin, Vladimir Dolgikh, Dmitry A. Arseniev, Alexander S. Kirpichnikov, Mikhail Gordeliy, Valentin Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria |
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Biological Sciences |
description |
Light-driven proton pumps are present in many organisms. Here, we present a high-resolution structure of a proteorhodopsin from a permafrost bacterium, Exiguobacterium sibiricum rhodopsin (ESR). Contrary to the proton pumps of known structure, ESR possesses three unique features. First, ESR's proton donor is a lysine side chain that is situated very close to the bulk solvent. Second, the α-helical structure in the middle of the helix F is replaced by 310- and π-helix–like elements that are stabilized by the Trp-154 and Asn-224 side chains. This feature is characteristic for the proteorhodopsin family of proteins. Third, the proton release region is connected to the bulk solvent by a chain of water molecules already in the ground state. Despite these peculiarities, the positions of water molecule and amino acid side chains in the immediate Schiff base vicinity are very well conserved. These features make ESR a very unusual proton pump. The presented structure sheds light on the large family of proteorhodopsins, for which structural information was not available previously. |
format |
Text |
author |
Gushchin, Ivan Chervakov, Pavel Kuzmichev, Pavel Popov, Alexander N. Round, Ekaterina Borshchevskiy, Valentin Ishchenko, Andrii Petrovskaya, Lada Chupin, Vladimir Dolgikh, Dmitry A. Arseniev, Alexander S. Kirpichnikov, Mikhail Gordeliy, Valentin |
author_facet |
Gushchin, Ivan Chervakov, Pavel Kuzmichev, Pavel Popov, Alexander N. Round, Ekaterina Borshchevskiy, Valentin Ishchenko, Andrii Petrovskaya, Lada Chupin, Vladimir Dolgikh, Dmitry A. Arseniev, Alexander S. Kirpichnikov, Mikhail Gordeliy, Valentin |
author_sort |
Gushchin, Ivan |
title |
Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria |
title_short |
Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria |
title_full |
Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria |
title_fullStr |
Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria |
title_full_unstemmed |
Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria |
title_sort |
structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria |
publisher |
National Academy of Sciences |
publishDate |
2013 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3732926 http://www.ncbi.nlm.nih.gov/pubmed/23872846 https://doi.org/10.1073/pnas.1221629110 |
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permafrost |
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permafrost |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3732926 http://www.ncbi.nlm.nih.gov/pubmed/23872846 http://dx.doi.org/10.1073/pnas.1221629110 |
op_doi |
https://doi.org/10.1073/pnas.1221629110 |
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Proceedings of the National Academy of Sciences |
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110 |
container_issue |
31 |
container_start_page |
12631 |
op_container_end_page |
12636 |
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1766166302331764736 |