Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I

Abstract Photosystem I (PS I) has a symmetric structure with two highly similar branches of pigments at the center that are involved in electron transfer, but shows very different efficiency along the two branches. We have determined the structure of cyanobacterial PS I at room temperature (RT) usin...

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Autores principales:	Stephen M. Keable, Adrian Kölsch, Philipp S. Simon, Medhanjali Dasgupta, Ruchira Chatterjee, Senthil Kumar Subramanian, Rana Hussein, Mohamed Ibrahim, In-Sik Kim, Isabel Bogacz, Hiroki Makita, Cindy C. Pham, Franklin D. Fuller, Sheraz Gul, Daniel Paley, Louise Lassalle, Kyle D. Sutherlin, Asmit Bhowmick, Nigel W. Moriarty, Iris D. Young, Johannes P. Blaschke, Casper de Lichtenberg, Petko Chernev, Mun Hon Cheah, Sehan Park, Gisu Park, Jangwoo Kim, Sang Jae Lee, Jaehyun Park, Kensuke Tono, Shigeki Owada, Mark S. Hunter, Alexander Batyuk, Roland Oggenfuss, Mathias Sander, Serhane Zerdane, Dmitry Ozerov, Karol Nass, Henrik Lemke, Roman Mankowsky, Aaron S. Brewster, Johannes Messinger, Nicholas K. Sauter, Vittal K. Yachandra, Junko Yano, Athina Zouni, Jan Kern
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/08b51738551f492bbef4bdd046b9396c
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spelling	oai:doaj.org-article:08b51738551f492bbef4bdd046b9396c2021-11-14T12:20:49ZRoom temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I10.1038/s41598-021-00236-32045-2322https://doaj.org/article/08b51738551f492bbef4bdd046b9396c2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-00236-3https://doaj.org/toc/2045-2322Abstract Photosystem I (PS I) has a symmetric structure with two highly similar branches of pigments at the center that are involved in electron transfer, but shows very different efficiency along the two branches. We have determined the structure of cyanobacterial PS I at room temperature (RT) using femtosecond X-ray pulses from an X-ray free electron laser (XFEL) that shows a clear expansion of the entire protein complex in the direction of the membrane plane, when compared to previous cryogenic structures. This trend was observed by complementary datasets taken at multiple XFEL beamlines. In the RT structure of PS I, we also observe conformational differences between the two branches in the reaction center around the secondary electron acceptors A1A and A1B. The π-stacked Phe residues are rotated with a more parallel orientation in the A-branch and an almost perpendicular confirmation in the B-branch, and the symmetry breaking PsaB-Trp673 is tilted and further away from A1A. These changes increase the asymmetry between the branches and may provide insights into the preferential directionality of electron transfer.Stephen M. KeableAdrian KölschPhilipp S. SimonMedhanjali DasguptaRuchira ChatterjeeSenthil Kumar SubramanianRana HusseinMohamed IbrahimIn-Sik KimIsabel BogaczHiroki MakitaCindy C. PhamFranklin D. FullerSheraz GulDaniel PaleyLouise LassalleKyle D. SutherlinAsmit BhowmickNigel W. MoriartyIris D. YoungJohannes P. BlaschkeCasper de LichtenbergPetko ChernevMun Hon CheahSehan ParkGisu ParkJangwoo KimSang Jae LeeJaehyun ParkKensuke TonoShigeki OwadaMark S. HunterAlexander BatyukRoland OggenfussMathias SanderSerhane ZerdaneDmitry OzerovKarol NassHenrik LemkeRoman MankowskyAaron S. BrewsterJohannes MessingerNicholas K. SauterVittal K. YachandraJunko YanoAthina ZouniJan KernNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Stephen M. Keable Adrian Kölsch Philipp S. Simon Medhanjali Dasgupta Ruchira Chatterjee Senthil Kumar Subramanian Rana Hussein Mohamed Ibrahim In-Sik Kim Isabel Bogacz Hiroki Makita Cindy C. Pham Franklin D. Fuller Sheraz Gul Daniel Paley Louise Lassalle Kyle D. Sutherlin Asmit Bhowmick Nigel W. Moriarty Iris D. Young Johannes P. Blaschke Casper de Lichtenberg Petko Chernev Mun Hon Cheah Sehan Park Gisu Park Jangwoo Kim Sang Jae Lee Jaehyun Park Kensuke Tono Shigeki Owada Mark S. Hunter Alexander Batyuk Roland Oggenfuss Mathias Sander Serhane Zerdane Dmitry Ozerov Karol Nass Henrik Lemke Roman Mankowsky Aaron S. Brewster Johannes Messinger Nicholas K. Sauter Vittal K. Yachandra Junko Yano Athina Zouni Jan Kern Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I
description	Abstract Photosystem I (PS I) has a symmetric structure with two highly similar branches of pigments at the center that are involved in electron transfer, but shows very different efficiency along the two branches. We have determined the structure of cyanobacterial PS I at room temperature (RT) using femtosecond X-ray pulses from an X-ray free electron laser (XFEL) that shows a clear expansion of the entire protein complex in the direction of the membrane plane, when compared to previous cryogenic structures. This trend was observed by complementary datasets taken at multiple XFEL beamlines. In the RT structure of PS I, we also observe conformational differences between the two branches in the reaction center around the secondary electron acceptors A1A and A1B. The π-stacked Phe residues are rotated with a more parallel orientation in the A-branch and an almost perpendicular confirmation in the B-branch, and the symmetry breaking PsaB-Trp673 is tilted and further away from A1A. These changes increase the asymmetry between the branches and may provide insights into the preferential directionality of electron transfer.
format	article
author	Stephen M. Keable Adrian Kölsch Philipp S. Simon Medhanjali Dasgupta Ruchira Chatterjee Senthil Kumar Subramanian Rana Hussein Mohamed Ibrahim In-Sik Kim Isabel Bogacz Hiroki Makita Cindy C. Pham Franklin D. Fuller Sheraz Gul Daniel Paley Louise Lassalle Kyle D. Sutherlin Asmit Bhowmick Nigel W. Moriarty Iris D. Young Johannes P. Blaschke Casper de Lichtenberg Petko Chernev Mun Hon Cheah Sehan Park Gisu Park Jangwoo Kim Sang Jae Lee Jaehyun Park Kensuke Tono Shigeki Owada Mark S. Hunter Alexander Batyuk Roland Oggenfuss Mathias Sander Serhane Zerdane Dmitry Ozerov Karol Nass Henrik Lemke Roman Mankowsky Aaron S. Brewster Johannes Messinger Nicholas K. Sauter Vittal K. Yachandra Junko Yano Athina Zouni Jan Kern
author_facet	Stephen M. Keable Adrian Kölsch Philipp S. Simon Medhanjali Dasgupta Ruchira Chatterjee Senthil Kumar Subramanian Rana Hussein Mohamed Ibrahim In-Sik Kim Isabel Bogacz Hiroki Makita Cindy C. Pham Franklin D. Fuller Sheraz Gul Daniel Paley Louise Lassalle Kyle D. Sutherlin Asmit Bhowmick Nigel W. Moriarty Iris D. Young Johannes P. Blaschke Casper de Lichtenberg Petko Chernev Mun Hon Cheah Sehan Park Gisu Park Jangwoo Kim Sang Jae Lee Jaehyun Park Kensuke Tono Shigeki Owada Mark S. Hunter Alexander Batyuk Roland Oggenfuss Mathias Sander Serhane Zerdane Dmitry Ozerov Karol Nass Henrik Lemke Roman Mankowsky Aaron S. Brewster Johannes Messinger Nicholas K. Sauter Vittal K. Yachandra Junko Yano Athina Zouni Jan Kern
author_sort	Stephen M. Keable
title	Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I
title_short	Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I
title_full	Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I
title_fullStr	Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I
title_full_unstemmed	Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I
title_sort	room temperature xfel crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem i
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/08b51738551f492bbef4bdd046b9396c
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Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I

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