9f9f: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: '''Unreleased structure''' The entry 9f9f is ON HOLD Authors: Bertrand, Q., Weinert, T., Standfuss, J. Description: Laser excitation effects on BR: Extrapolated 6 ps Light dataset reco...
 
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 9f9f is ON HOLD
==Laser excitation effects on BR: Extrapolated 6 ps Light dataset recorded at 2493 GW/cm2 at SwissFEL==
<StructureSection load='9f9f' size='340' side='right'caption='[[9f9f]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9f9f]] 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=9F9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9F9F FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=9f9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9f9f OCA], [https://pdbe.org/9f9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9f9f RCSB], [https://www.ebi.ac.uk/pdbsum/9f9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9f9f ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Time-resolved serial crystallography at X-ray Free Electron Lasers offers the opportunity to observe ultrafast photochemical reactions at the atomic level. The technique has yielded exciting molecular insights into various biological processes including light sensing and photochemical energy conversion. However, to achieve sufficient levels of activation within an optically dense crystal, high laser power densities are often used, which has led to an ongoing debate to which extent photodamage may compromise interpretation of the results. Here we compare time-resolved serial crystallographic data of the bacteriorhodopsin K-intermediate collected at laser power densities ranging from 0.04 to 2493 GW/cm(2) and follow energy dissipation of the absorbed photons logarithmically from picoseconds to milliseconds. Although the effects of high laser power densities on the overall structure are small, in the upper excitation range we observe significant changes in retinal conformation and increased heating of the functionally critical counterion cluster. We compare light-activation within crystals to that in solution and discuss the impact of the observed changes on bacteriorhodopsin biology.


Authors: Bertrand, Q., Weinert, T., Standfuss, J.
Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate.,Bertrand Q, Nogly P, Nango E, Kekilli D, Khusainov G, Furrer A, James D, Dworkowski F, Skopintsev P, Mous S, Martiel I, Borjesson P, Ortolani G, Huang CY, Kepa M, Ozerov D, Brunle S, Panneels V, Tanaka T, Tanaka R, Tono K, Owada S, Johnson PJM, Nass K, Knopp G, Cirelli C, Milne C, Schertler G, Iwata S, Neutze R, Weinert T, Standfuss J Nat Commun. 2024 Nov 27;15(1):10278. doi: 10.1038/s41467-024-54422-8. PMID:39604356<ref>PMID:39604356</ref>


Description: Laser excitation effects on BR: Extrapolated 6 ps Light dataset recorded at 2493 GW/cm2 at SwissFEL
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Bertrand, Q]]
<div class="pdbe-citations 9f9f" style="background-color:#fffaf0;"></div>
[[Category: Weinert, T]]
== References ==
[[Category: Standfuss, J]]
<references/>
__TOC__
</StructureSection>
[[Category: Halobacterium salinarum]]
[[Category: Large Structures]]
[[Category: Bertrand Q]]
[[Category: Standfuss J]]
[[Category: Weinert T]]

Latest revision as of 13:21, 22 January 2025

Laser excitation effects on BR: Extrapolated 6 ps Light dataset recorded at 2493 GW/cm2 at SwissFELLaser excitation effects on BR: Extrapolated 6 ps Light dataset recorded at 2493 GW/cm2 at SwissFEL

Structural highlights

9f9f is a 1 chain structure with sequence from Halobacterium salinarum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BACR_HALSA Light-driven proton pump.

Publication Abstract from PubMed

Time-resolved serial crystallography at X-ray Free Electron Lasers offers the opportunity to observe ultrafast photochemical reactions at the atomic level. The technique has yielded exciting molecular insights into various biological processes including light sensing and photochemical energy conversion. However, to achieve sufficient levels of activation within an optically dense crystal, high laser power densities are often used, which has led to an ongoing debate to which extent photodamage may compromise interpretation of the results. Here we compare time-resolved serial crystallographic data of the bacteriorhodopsin K-intermediate collected at laser power densities ranging from 0.04 to 2493 GW/cm(2) and follow energy dissipation of the absorbed photons logarithmically from picoseconds to milliseconds. Although the effects of high laser power densities on the overall structure are small, in the upper excitation range we observe significant changes in retinal conformation and increased heating of the functionally critical counterion cluster. We compare light-activation within crystals to that in solution and discuss the impact of the observed changes on bacteriorhodopsin biology.

Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate.,Bertrand Q, Nogly P, Nango E, Kekilli D, Khusainov G, Furrer A, James D, Dworkowski F, Skopintsev P, Mous S, Martiel I, Borjesson P, Ortolani G, Huang CY, Kepa M, Ozerov D, Brunle S, Panneels V, Tanaka T, Tanaka R, Tono K, Owada S, Johnson PJM, Nass K, Knopp G, Cirelli C, Milne C, Schertler G, Iwata S, Neutze R, Weinert T, Standfuss J Nat Commun. 2024 Nov 27;15(1):10278. doi: 10.1038/s41467-024-54422-8. PMID:39604356[1]

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

References

  1. ↑ Bertrand Q, Nogly P, Nango E, Kekilli D, Khusainov G, Furrer A, James D, Dworkowski F, Skopintsev P, Mous S, Martiel I, Börjesson P, Ortolani G, Huang CY, Kepa M, Ozerov D, Brünle S, Panneels V, Tanaka T, Tanaka R, Tono K, Owada S, Johnson PJM, Nass K, Knopp G, Cirelli C, Milne C, Schertler G, Iwata S, Neutze R, Weinert T, Standfuss J. Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate. Nat Commun. 2024 Nov 27;15(1):10278. PMID:39604356 doi:10.1038/s41467-024-54422-8

9f9f, resolution 1.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=9f9f&oldid=4252000"