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[[Image: | ==Crystal structure of bacteriorhodopsin mutant L94A crystallized from bicelles== | ||
<StructureSection load='3hao' size='340' side='right' caption='[[3hao]], [[Resolution|resolution]] 2.49Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3hao]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HAO FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RET:RETINAL'>RET</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3han|3han]], [[3hap|3hap]], [[3haq|3haq]], [[3har|3har]], [[3has|3has]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bop, VNG_1467G ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 Halobacterium salinarum])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hao OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hao RCSB], [http://www.ebi.ac.uk/pdbsum/3hao PDBsum]</span></td></tr> | |||
<table> | |||
== 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/ha/3hao_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins. | |||
Similar energetic contributions of packing in the core of membrane and water-soluble proteins.,Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754<ref>PMID:19603754</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Bacteriorhodopsin|Bacteriorhodopsin]] | *[[Bacteriorhodopsin|Bacteriorhodopsin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Bowie, J U.]] | [[Category: Bowie, J U.]] | ||
Revision as of 13:54, 29 September 2014
Crystal structure of bacteriorhodopsin mutant L94A crystallized from bicellesCrystal structure of bacteriorhodopsin mutant L94A crystallized from bicelles
Structural highlights
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 PubMedA major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins. Similar energetic contributions of packing in the core of membrane and water-soluble proteins.,Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Halobacterium salinarum
- Bowie, J U.
- Joh, N H.
- Yang, D.
- Bacteriorhodopsin
- Cell membrane
- Chromophore
- Evolutionary constraint
- Helical membrane protein
- Hydrogen ion transport
- Integral membrane protein
- Ion transport
- Membrane
- Membrane protein
- Packing force
- Photoreceptor protein
- Proton transport
- Pyrrolidone carboxylic acid
- Receptor
- Retinal protein
- Sensory transduction
- Transmembrane
- Transport
- Transport protein
- Van der waal