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==Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 8.3 ms state structure==
==Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 8.3 ms state structure==
<StructureSection load='6g7l' size='340' side='right' caption='[[6g7l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6g7l' size='340' side='right'caption='[[6g7l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6g7l]] is a 1 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=6G7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G7L FirstGlance]. <br>
<table><tr><td colspan='2'>[[6g7l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum_NRC-1 Halobacterium salinarum NRC-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G7L FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=6g7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g7l OCA], [http://pdbe.org/6g7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g7l RCSB], [http://www.ebi.ac.uk/pdbsum/6g7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g7l ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <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=6g7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g7l OCA], [https://pdbe.org/6g7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g7l RCSB], [https://www.ebi.ac.uk/pdbsum/6g7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g7l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump.  
[https://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 ==
Line 18: Line 19:
</div>
</div>
<div class="pdbe-citations 6g7l" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6g7l" style="background-color:#fffaf0;"></div>
==See Also==
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Halsa]]
[[Category: Halobacterium salinarum NRC-1]]
[[Category: Barty, A]]
[[Category: Large Structures]]
[[Category: Bath, P]]
[[Category: Barty A]]
[[Category: Borin, V]]
[[Category: Bath P]]
[[Category: Bosman, R]]
[[Category: Borin V]]
[[Category: Bruenle, S]]
[[Category: Bosman R]]
[[Category: Cabajo, S]]
[[Category: Bruenle S]]
[[Category: Furrer, A]]
[[Category: Cabajo S]]
[[Category: Gashi, D]]
[[Category: Furrer A]]
[[Category: Hunter, M]]
[[Category: Gashi D]]
[[Category: Iwata, S]]
[[Category: Hunter M]]
[[Category: Jaeger, K]]
[[Category: Iwata S]]
[[Category: James, D]]
[[Category: Jaeger K]]
[[Category: Kekilli, D]]
[[Category: James D]]
[[Category: Koglin, J]]
[[Category: Kekilli D]]
[[Category: Lane, T]]
[[Category: Koglin J]]
[[Category: Milne, C]]
[[Category: Lane T]]
[[Category: Nango, E]]
[[Category: Milne C]]
[[Category: Nass, K]]
[[Category: Nango E]]
[[Category: Neutze, R]]
[[Category: Nass K]]
[[Category: Nogly, P]]
[[Category: Neutze R]]
[[Category: Ozerov, D]]
[[Category: Nogly P]]
[[Category: Panneels, V]]
[[Category: Ozerov D]]
[[Category: Schapiro, I]]
[[Category: Panneels V]]
[[Category: Schertler, G]]
[[Category: Schapiro I]]
[[Category: Seaberg, M]]
[[Category: Schertler G]]
[[Category: Skopintsev, P]]
[[Category: Seaberg M]]
[[Category: Standfuss, J]]
[[Category: Skopintsev P]]
[[Category: Tanaka, T]]
[[Category: Standfuss J]]
[[Category: Weierstall, U]]
[[Category: Tanaka T]]
[[Category: Weinert, T]]
[[Category: Weierstall U]]
[[Category: White, T]]
[[Category: Weinert T]]
[[Category: Wu, W]]
[[Category: White T]]
[[Category: Femtosecond]]
[[Category: Wu W]]
[[Category: Proton transport]]
[[Category: Retinal isomerization]]
[[Category: Room temperature]]
[[Category: Time resolved crystallography]]
[[Category: Ultrafast]]

Latest revision as of 10:58, 17 October 2024

Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 8.3 ms state structureRetinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 8.3 ms state structure

Structural highlights

6g7l is a 1 chain structure with sequence from Halobacterium salinarum NRC-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BACR_HALSA Light-driven proton pump.

Publication Abstract from PubMed

Ultrafast isomerization of retinal is the primary step in photoresponsive biological functions including vision in humans and ion-transport across bacterial membranes. We studied the sub-picosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin using an x-ray laser. A series of structural snapshots with near-atomic spatial and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket prior to passing through a twisted geometry and emerging in the 13-cis conformation. Our findings suggest ultrafast collective motions of aspartic acid residues and functional water molecules in the proximity of the retinal Schiff base as a key ingredient for this stereo-selective and efficient photochemical reaction.

Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser.,Nogly P, Weinert T, James D, Carbajo S, Ozerov D, Furrer A, Gashi D, Borin V, Skopintsev P, Jaeger K, Nass K, Bath P, Bosman R, Koglin J, Seaberg M, Lane T, Kekilli D, Brunle S, Tanaka T, Wu W, Milne C, White T, Barty A, Weierstall U, Panneels V, Nango E, Iwata S, Hunter M, Schapiro I, Schertler G, Neutze R, Standfuss J Science. 2018 Jun 14. pii: science.aat0094. doi: 10.1126/science.aat0094. PMID:29903883[1]

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

See Also

References

  1. ↑ Nogly P, Weinert T, James D, Carbajo S, Ozerov D, Furrer A, Gashi D, Borin V, Skopintsev P, Jaeger K, Nass K, Bath P, Bosman R, Koglin J, Seaberg M, Lane T, Kekilli D, Brunle S, Tanaka T, Wu W, Milne C, White T, Barty A, Weierstall U, Panneels V, Nango E, Iwata S, Hunter M, Schapiro I, Schertler G, Neutze R, Standfuss J. Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science. 2018 Jun 14. pii: science.aat0094. doi: 10.1126/science.aat0094. PMID:29903883 doi:http://dx.doi.org/10.1126/science.aat0094

6g7l, resolution 1.90Å

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