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000059154 0247_ $$2DOI$$a10.1562/2006-06-23-RA-947
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000059154 084__ $$2WoS$$aBiochemistry & Molecular Biology
000059154 084__ $$2WoS$$aBiophysics
000059154 1001_ $$0P:(DE-HGF)0$$aGmelin, W.$$b0
000059154 245__ $$aThe Crystal Structure of the L1 Intermediate of Halorhodopsin at 1.9 Å Resolution
000059154 260__ $$aMalden, Mass.$$bWiley-Blackwell$$c2007
000059154 300__ $$a369 - 377
000059154 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000059154 440_0 $$015281$$aPhotochemistry and Photobiology$$v83$$x0031-8655
000059154 500__ $$aRecord converted from VDB: 12.11.2012
000059154 520__ $$aThe mutant T203V of the light driven chloride pump halorhodopsin from Halobacterium salinarum was crystallized and the X-ray structure was solved at 1.6 angstroms resolution. The T203V structure turned out to be nearly identical to the wild type protein with a root mean square deviation of 0.43 angstroms for the carbon alpha atoms of the protein backbone. Two chloride binding (CB) sites were demonstrated by a substitution of chloride with bromide and an analysis of anomalous difference Fourier maps. The CB1 site was found at the same position as in the wild type structure. In addition, a second chloride binding site CB2 was identified around Q105 due to higher resolution in the mutant crystal. As T203V showed a 10 times slower decay of its photocycle intermediate L, this intermediate could be trapped with an occupancy of 60% upon illumination at room temperature and subsequent cooling to 120 degrees K. Fourier transform infrared spectroscopy clearly identified the crystal to be trapped in the L1 intermediate state and the X-ray structure was solved to 1.9 angstroms resolution. In this intermediate, the chloride moved by 0.3 angstroms within binding site CB1 as indicated by peaks in difference Fourier density maps. The chloride in the second binding site CB2 remained unchanged. Thus, intraproteinous chloride translocation from the extracellular to the cytoplasmic part of the protein must occur in reaction steps following the L1 intermediate in the catalytic cycle of halorhodopsin.
000059154 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000059154 650_2 $$2MeSH$$aAmino Acid Substitution
000059154 650_2 $$2MeSH$$aBinding Sites
000059154 650_2 $$2MeSH$$aChlorides: chemistry
000059154 650_2 $$2MeSH$$aCrystallography, X-Ray
000059154 650_2 $$2MeSH$$aHalobacterium salinarum: chemistry
000059154 650_2 $$2MeSH$$aHalobacterium salinarum: genetics
000059154 650_2 $$2MeSH$$aHalobacterium salinarum: radiation effects
000059154 650_2 $$2MeSH$$aHalorhodopsins: chemistry
000059154 650_2 $$2MeSH$$aHalorhodopsins: genetics
000059154 650_2 $$2MeSH$$aHalorhodopsins: radiation effects
000059154 650_2 $$2MeSH$$aModels, Molecular
000059154 650_2 $$2MeSH$$aMutagenesis, Site-Directed
000059154 650_2 $$2MeSH$$aPhotochemistry
000059154 650_7 $$00$$2NLM Chemicals$$aChlorides
000059154 650_7 $$00$$2NLM Chemicals$$aHalorhodopsins
000059154 650_7 $$2WoSType$$aJ
000059154 7001_ $$0P:(DE-HGF)0$$aZeth, K.$$b1
000059154 7001_ $$0P:(DE-Juel1)VDB4616$$aEfremov, R.$$b2$$uFZJ
000059154 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b3$$uFZJ
000059154 7001_ $$0P:(DE-HGF)0$$aTittor, J.$$b4
000059154 7001_ $$0P:(DE-HGF)0$$aOesterhelt, D.$$b5
000059154 773__ $$0PERI:(DE-600)2048860-9$$a10.1562/2006-06-23-RA-947$$gVol. 83, p. 369 - 377$$p369 - 377$$q83<369 - 377$$tPhotochemistry and photobiology$$v83$$x0031-8655$$y2007
000059154 8567_ $$uhttp://dx.doi.org/10.1562/2006-06-23-RA-947
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000059154 9141_ $$y2007
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