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1qm8

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Revision as of 12:35, 10 September 2015

STRUCTURE OF BACTERIORHODOPSIN AT 100 K

Structural highlights

1qm8 is a 1 chain structure with sequence from Halobacterium salinarum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , ,
Related:	1c3w, 1brd, 2brd, 1brr, 1bac, 1bad, 1bha, 1bhb, 1bct, 1ap9, 1at9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[BACR_HALSA] Light-driven proton pump.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

When the two-dimensional crystal of bacteriorhodopsin (bR), purple membrane, is incubated at high temperature (32 degreesC) with a small amount of the neutral detergent octylthioglucoside in the presence of the precipitant ammonium sulfate, a large fraction of the membrane fragments is converted into spherical vesicles with a diameter of 50 nm, which are able to assemble into optically isotropic hexagonal crystals when the precipitant concentration is increased. The vesicularization of purple membrane takes place under such a condition that the miscibility of the detergent to the aqueous phase becomes very low, and we suggest that it is initiated by insertion of the detergent molecules into the membrane. At low temperature, the transformation into the vesicular structure is inhibited and no large crystal is produced directly from membrane/detergent/precipitant mixtures. When a suspension of the spherical vesicles produced at the high temperature is cooled and concentrated below 15 degreesC, however, a birefringent hexagonal crystal is produced that diffracts X-rays beyond 2.5 A resolution. This new crystal belongs to the space group P622 with unit cell dimensions of a=b=104.7 A and c=114.1 A, and it is shown to be made up of stacked planar membranes, in each of which the bR trimers are arranged on a honeycomb lattice and the space among the proteins is filled with the detergent molecules and native lipids. These stacked membranes are suggested to be produced by successive fusion of the spherical vesicles. This implies that the crystallization is achieved without any step for complete solubilization of the protein. The present result offers a unique crystallization method that may be applicable to such membrane proteins that are liable to denature in the presence of an excess amount of detergent.

A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies.,Takeda K, Sato H, Hino T, Kono M, Fukuda K, Sakurai I, Okada T, Kouyama T J Mol Biol. 1998 Oct 23;283(2):463-74. PMID:9769218^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Takeda K, Sato H, Hino T, Kono M, Fukuda K, Sakurai I, Okada T, Kouyama T. A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. J Mol Biol. 1998 Oct 23;283(2):463-74. PMID:9769218 doi:S0022-2836(98)92103-9

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qm8"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=L1P:3-PHOSPHORYL-[1,2-DI-PHYTANYL]GLYCEROL'>L1P</scene>, <scene name='pdbligand=L2P:2,3-DI-PHYTANYL-GLYCEROL'>L2P</scene>, <scene name='pdbligand=L3P:2,3-DI-O-PHYTANLY-3-SN-GLYCERO-1-PHOSPHORYL-3-SN-GLYCEROL-1-PHOSPHATE'>L3P</scene>, <scene name='pdbligand=L4P:3-[GLYCEROLYLPHOSPHONYL]-[1,2-DI-PHYTANYL]GLYCEROL'>L4P</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c3w|1c3w]], [[1brd|1brd]], [[2brd|2brd]], [[1brr|1brr]], [[1bac|1bac]], [[1bad|1bad]], [[1bha|1bha]], [[1bhb|1bhb]], [[1bct|1bct]], [[1ap9|1ap9]], [[1at9|1at9]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qm8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qm8 RCSB], [http://www.ebi.ac.uk/pdbsum/1qm8 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qm8 OCA], [http://pdbe.org/1qm8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qm8 RCSB], [http://www.ebi.ac.uk/pdbsum/1qm8 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1qm8" style="background-color:#fffaf0;"></div>
 ==See Also==

1qm8

From Proteopedia

Revision as of 12:35, 10 September 2015

STRUCTURE OF BACTERIORHODOPSIN AT 100 K

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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