3utx: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3utx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Halsa Halsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTX FirstGlance]. <br> | <table><tr><td colspan='2'>[[3utx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Halsa Halsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTX FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3utv|3utv]], [[3utw|3utw]], [[3uty|3uty]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3utv|3utv]], [[3utw|3utw]], [[3uty|3uty]]</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=64091 HALSA])</td></tr> | <tr id='gene'><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=64091 HALSA])</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=3utx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3utx RCSB], [http://www.ebi.ac.uk/pdbsum/3utx 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=3utx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3utx RCSB], [http://www.ebi.ac.uk/pdbsum/3utx PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Halsa]] | [[Category: Halsa]] | ||
[[Category: Bowie, J U | [[Category: Bowie, J U]] | ||
[[Category: Cao, Z | [[Category: Cao, Z]] | ||
[[Category: Ion transport]] | [[Category: Ion transport]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 20:13, 24 December 2014
Crystal structure of bacteriorhodopsin mutant T46ACrystal structure of bacteriorhodopsin mutant T46A
Structural highlights
Function[BACR_HALSA] Light-driven proton pump. Publication Abstract from PubMedThe intricate functions of membrane proteins would not be possible without bends or breaks that are remarkably common in transmembrane helices. The frequent helix distortions are nevertheless surprising because backbone hydrogen bonds should be strong in an apolar membrane, potentially rigidifying helices. It is therefore mysterious how distortions can be generated by the evolutionary currency of random point mutations. Here we show that we can engineer a transition between distinct distorted helix conformations in bacteriorhodopsin with a single-point mutation. Moreover, we estimate the energetic cost of the conformational transitions to be smaller than 1 kcal/mol. We propose that the low energy of distortion is explained in part by the shifting of backbone hydrogen bonding partners. Consistent with this view, extensive backbone hydrogen bond shifts occur during helix conformational changes that accompany functional cycles. Our results explain how evolution has been able to liberally exploit transmembrane helix bending for the optimization of membrane protein structure, function, and dynamics. Shifting hydrogen bonds may produce flexible transmembrane helices.,Cao Z, Bowie JU Proc Natl Acad Sci U S A. 2012 May 22;109(21):8121-6. Epub 2012 May 7. PMID:22566663[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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