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000202104 1001_ $$0P:(DE-Juel1)165798$$aGushchin, Ivan$$b0$$ufzj
000202104 245__ $$aStructural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria
000202104 260__ $$aWashington, DC$$bNational Acad. of Sciences$$c2013
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000202104 520__ $$aLight-driven proton pumps are present in many organisms. Here, we present a high-resolution structure of a proteorhodopsin from a permafrost bacterium, Exiguobacterium sibiricum rhodopsin (ESR). Contrary to the proton pumps of known structure, ESR possesses three unique features. First, ESR's proton donor is a lysine side chain that is situated very close to the bulk solvent. Second, the α-helical structure in the middle of the helix F is replaced by 3(10)- and π-helix-like elements that are stabilized by the Trp-154 and Asn-224 side chains. This feature is characteristic for the proteorhodopsin family of proteins. Third, the proton release region is connected to the bulk solvent by a chain of water molecules already in the ground state. Despite these peculiarities, the positions of water molecule and amino acid side chains in the immediate Schiff base vicinity are very well conserved. These features make ESR a very unusual proton pump. The presented structure sheds light on the large family of proteorhodopsins, for which structural information was not available previously.
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000202104 650_7 $$2NLM Chemicals$$aBacterial Proteins
000202104 650_7 $$2NLM Chemicals$$aproteorhodopsin
000202104 650_7 $$09009-81-8$$2NLM Chemicals$$aRhodopsin
000202104 7001_ $$0P:(DE-Juel1)157749$$aChervakov, Pavel$$b1$$ufzj
000202104 7001_ $$0P:(DE-HGF)0$$aKuzmichev, Pavel$$b2
000202104 7001_ $$0P:(DE-HGF)0$$aPopov, Alexander N$$b3
000202104 7001_ $$0P:(DE-HGF)0$$aRound, Ekaterina$$b4
000202104 7001_ $$0P:(DE-Juel1)144613$$aBorshchevskiy, Valentin$$b5
000202104 7001_ $$0P:(DE-Juel1)131968$$aIshchenko, Andrii$$b6
000202104 7001_ $$0P:(DE-HGF)0$$aPetrovskaya, Lada$$b7
000202104 7001_ $$0P:(DE-HGF)0$$aChupin, Vladimir$$b8
000202104 7001_ $$0P:(DE-HGF)0$$aDolgikh, Dmitry A$$b9
000202104 7001_ $$0P:(DE-HGF)0$$aArseniev, Alexander S$$b10
000202104 7001_ $$0P:(DE-HGF)0$$aArseniev, Alexander A$$b11
000202104 7001_ $$0P:(DE-HGF)0$$aKirpichnikov, Mikhail$$b12
000202104 7001_ $$0P:(DE-Juel1)131964$$aGordeliy, Valentin$$b13$$eCorresponding Author$$ufzj
000202104 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.1221629110$$gVol. 110, no. 31, p. 12631 - 12636$$n31$$p12631 - 12636$$tProceedings of the National Academy of Sciences of the United States of America$$v110$$x1091-6490$$y2013
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