View source for 1bha


==THREE-DIMENSIONAL STRUCTURE OF (1-71) BACTERIOOPSIN SOLUBILIZED IN METHANOL-CHLOROFORM AND SDS MICELLES DETERMINED BY 15N-1H HETERONUCLEAR NMR SPECTROSCOPY==
<StructureSection load='1bha' size='340' side='right'caption='[[1bha]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bha]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bha OCA], [https://pdbe.org/1bha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bha RCSB], [https://www.ebi.ac.uk/pdbsum/1bha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bha ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bha_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bha ConSurf].
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== Publication Abstract from PubMed ==
Spatial structures of a chymotryptic fragment C2 (residues 1-71) of bacterioopsin from Halobacterium halobium, solubilized in a mixture of methanol/chloroform (1:1, by vol.) and 0.1 M 2HCO2NH4, or in perdeuterated sodium (2H)dodecyl sulfate (SDS) micelles in the presence of perdeuterated (2,2,2-2H)trifluoroethanol, were determined by two-dimensional and three-dimensional heteronuclear 15N-1H NMR techniques. The influence of (2,2,2-2H)trifluoroethanol on the conformational dynamics of C2 in micelles and the effect of the salt (organic mixture) were studied. Under the best conditions, 1H and 15N resonances of 15N-uniformly enriched protein were assigned in both milieus by homonuclear two-dimensional NOE (NOESY) and two-dimensional total-correlated (TOCSY) spectra and heteronuclear three-dimensional NOESY-multiple-quantum-correlation (HMQC) and TOCSY-HMQC spectra. 651 (organic mixture) and 520 (micelles) interproton-distance constraints, derived from volumes of cross-peaks in two-dimensional NOESY and three-dimensional NOESY-HMQC spectra, along with deuterium exchange rates of amide groups measured in both milieus and 51 HN-C alpha H coupling constants obtained in the case of the organic mixture, were used in the construction of C2 spatial structures. Obtained structures are similar in both milieus and have two right-handed alpha-helical regions stretching from Pro8 to Met32 and Phe42 to Tyr64 (organic mixture), and from Pro8 to Met32 and Ala39 to Leu62 (micelles). In micelles, the second alpha helix is terminated by C-cap Gly63, adopting a conformation characteristic of a left-handed helix. Residues Gly65 to Thr67 from the turn of a right-handed helix. In the isotropic medium of the organic mixture, the C-terminal region of residues 65-71 lacks an ordered structure. Torsion angles chi 1 were unequivocally determined for 18 alpha-helical residues in both milieus. In the isotropic organic mixture and anisotropic micellar system, C2 remains a compact structure with a characteristic size of 3.0-3.5 nm. C2 seems to be present in at least two conformational states, packed and unpacked. Using NMR data, along with the electron cryomicroscopy model of bacteriorhodopsin [Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckman, E. &amp; Downing, K. H. (1990) J. Mol. Biol. 213, 899-929], we suggested a model for the conformation of C2 in this putative close-packed state. However, no NOE contact between alpha helices was found in either milieu.

Three-dimensional structure of (1-71)bacterioopsin solubilized in methanol/chloroform and SDS micelles determined by 15N-1H heteronuclear NMR spectroscopy.,Pervushin KV, Orekhov VYu, Popov AI, Musina LYu, Arseniev AS Eur J Biochem. 1994 Jan 15;219(1-2):571-83. PMID:8307023<ref>PMID:8307023</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Halobacterium salinarum]]
[[Category: Large Structures]]
[[Category: Arseniev AS]]
[[Category: Musina LY]]
[[Category: Orekhov VY]]
[[Category: Pervushin KV]]
[[Category: Popov AI]]