1tn0: Difference between revisions
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<StructureSection load='1tn0' size='340' side='right'caption='[[1tn0]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1tn0' size='340' side='right'caption='[[1tn0]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1tn0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1tn0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TN0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RET:RETINAL'>RET</scene></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=1tn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tn0 OCA], [https://pdbe.org/1tn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tn0 ProSAT]</span></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=1tn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tn0 OCA], [https://pdbe.org/1tn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tn0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Halobacterium salinarum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boulting | [[Category: Boulting G]] | ||
[[Category: Bowie | [[Category: Bowie JU]] | ||
[[Category: Faham | [[Category: Faham S]] | ||
[[Category: Whitelegge | [[Category: Whitelegge J]] | ||
[[Category: Yang | [[Category: Yang D]] | ||
[[Category: Yohannan | [[Category: Yohannan S]] | ||
Latest revision as of 09:32, 23 August 2023
Structure of bacterorhodopsin mutant A51PStructure of bacterorhodopsin mutant A51P
Structural highlights
FunctionBACR_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 PubMedProline residues are relatively common in transmembrane helices. This suggests that proline substitutions may be readily tolerated in membrane proteins, even though they invariably produce deviations from canonical helical structure. We have experimentally tested this possibility by making proline substitutions at 15 positions throughout the N-terminal half of bacteriorhodopsin helix B. We find that six of the substitutions yielded no active protein and all the others were destabilizing. Three mutations were only slightly destabilizing, however, reducing stability by about 0.5 kcal/mol, and these all occurred close to the N terminus. This result is consistent with the observation that proline is more common near the ends of TM helices. To learn how proline side-chains could be structurally accommodated at different locations in the helix, we solved the structures of a moderately destabilized mutant positioned near the N terminus of the helix, K41P, and a severely destabilized mutant positioned near the middle of the helix, A51P. The K41P mutation produced only local structural alterations, while the A51P mutation resulted in small, but widely distributed structural changes in helix B. Our results indicate that proline is not easily accommodated in transmembrane helices and that the tolerance to proline substitution is dependent, in a complex way, on the position in the structure. Proline substitutions are not easily accommodated in a membrane protein.,Yohannan S, Yang D, Faham S, Boulting G, Whitelegge J, Bowie JU J Mol Biol. 2004 Jul 30;341(1):1-6. PMID:15312757[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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