7z09: Difference between revisions
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==Crystal structure of the ground state of bacteriorhodopsin at 1.05 Angstrom resolution== | ==Crystal structure of the ground state of bacteriorhodopsin at 1.05 Angstrom resolution== | ||
<StructureSection load='7z09' size='340' side='right'caption='[[7z09]]' scene=''> | <StructureSection load='7z09' size='340' side='right'caption='[[7z09]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z09 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7z09]] is a 1 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=7Z09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z09 FirstGlance]. <br> | ||
</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=7z09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z09 OCA], [https://pdbe.org/7z09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z09 RCSB], [https://www.ebi.ac.uk/pdbsum/7z09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z09 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYR:N~6~-[(2Z,4E,6E,8E)-3,7-DIMETHYL-9-(2,6,6-TRIMETHYLCYCLOHEX-1-EN-1-YL)NONA-2,4,6,8-TETRAENYL]LYSINE'>LYR</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=7z09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z09 OCA], [https://pdbe.org/7z09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z09 RCSB], [https://www.ebi.ac.uk/pdbsum/7z09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z09 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hydrogen bonds are fundamental to the structure and function of biological macromolecules and have been explored in detail. The chains of hydrogen bonds (CHBs) and low-barrier hydrogen bonds (LBHBs) were proposed to play essential roles in enzyme catalysis and proton transport. However, high-resolution structural data from CHBs and LBHBs is limited. The challenge is that their 'visualization' requires ultrahigh-resolution structures of the ground and functionally important intermediate states to identify proton translocation events and perform their structural assignment. Our true-atomic-resolution structures of the light-driven proton pump bacteriorhodopsin, a model in studies of proton transport, show that CHBs and LBHBs not only serve as proton pathways, but also are indispensable for long-range communications, signaling and proton storage in proteins. The complete picture of CHBs and LBHBs discloses their multifunctional roles in providing protein functions and presents a consistent picture of proton transport and storage resolving long-standing debates and controversies. | |||
True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins.,Borshchevskiy V, Kovalev K, Round E, Efremov R, Astashkin R, Bourenkov G, Bratanov D, Balandin T, Chizhov I, Baeken C, Gushchin I, Kuzmin A, Alekseev A, Rogachev A, Willbold D, Engelhard M, Bamberg E, Buldt G, Gordeliy V Nat Struct Mol Biol. 2022 Apr 28. pii: 10.1038/s41594-022-00762-2. doi:, 10.1038/s41594-022-00762-2. PMID:35484235<ref>PMID:35484235</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7z09" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Halobacterium salinarum]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Borshchevskiy V]] | [[Category: Borshchevskiy, V]] | ||
[[Category: Bourenkov G]] | [[Category: Bourenkov, G]] | ||
[[Category: Efremov R]] | [[Category: Efremov, R]] | ||
[[Category: Gordeliy V]] | [[Category: Gordeliy, V]] | ||
[[Category: Kovalev K]] | [[Category: Kovalev, K]] | ||
[[Category: Round E]] | [[Category: Round, E]] | ||
[[Category: Ion transport]] | |||
[[Category: Membrane protein]] | |||
[[Category: Microbial rhodopsin]] | |||
[[Category: Photocycle]] | |||
[[Category: Proton pump]] | |||
[[Category: Retinal]] | |||
[[Category: Rhodopsin]] | |||
[[Category: Ultrahigh resolution]] | |||
Revision as of 09:38, 12 May 2022
Crystal structure of the ground state of bacteriorhodopsin at 1.05 Angstrom resolutionCrystal structure of the ground state of bacteriorhodopsin at 1.05 Angstrom resolution
Structural highlights
Function[BACR_HALSA] Light-driven proton pump. Publication Abstract from PubMedHydrogen bonds are fundamental to the structure and function of biological macromolecules and have been explored in detail. The chains of hydrogen bonds (CHBs) and low-barrier hydrogen bonds (LBHBs) were proposed to play essential roles in enzyme catalysis and proton transport. However, high-resolution structural data from CHBs and LBHBs is limited. The challenge is that their 'visualization' requires ultrahigh-resolution structures of the ground and functionally important intermediate states to identify proton translocation events and perform their structural assignment. Our true-atomic-resolution structures of the light-driven proton pump bacteriorhodopsin, a model in studies of proton transport, show that CHBs and LBHBs not only serve as proton pathways, but also are indispensable for long-range communications, signaling and proton storage in proteins. The complete picture of CHBs and LBHBs discloses their multifunctional roles in providing protein functions and presents a consistent picture of proton transport and storage resolving long-standing debates and controversies. True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins.,Borshchevskiy V, Kovalev K, Round E, Efremov R, Astashkin R, Bourenkov G, Bratanov D, Balandin T, Chizhov I, Baeken C, Gushchin I, Kuzmin A, Alekseev A, Rogachev A, Willbold D, Engelhard M, Bamberg E, Buldt G, Gordeliy V Nat Struct Mol Biol. 2022 Apr 28. pii: 10.1038/s41594-022-00762-2. doi:, 10.1038/s41594-022-00762-2. PMID:35484235[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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