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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) 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 A_1A and A_1B. 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 A_1A. These changes increase the asymmetry between the branches and may provide insights into the preferential directionality of electron transfer.

SUBMITTER: Keable SM

PROVIDER: S-EPMC8575901 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature

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

Keable Stephen M SM Kölsch Adrian A Simon Philipp S PS Dasgupta Medhanjali M Chatterjee Ruchira R Subramanian Senthil Kumar SK Hussein Rana R Ibrahim Mohamed M Kim In-Sik IS Bogacz Isabel I Makita Hiroki H Pham Cindy C CC Fuller Franklin D FD Gul Sheraz S Paley Daniel D Lassalle Louise L Sutherlin Kyle D KD Bhowmick Asmit A Moriarty Nigel W NW Young Iris D ID Blaschke Johannes P JP de Lichtenberg Casper C Chernev Petko P Cheah Mun Hon MH Park Sehan S Park Gisu G Kim Jangwoo J Lee Sang Jae SJ Park Jaehyun J Tono Kensuke K Owada Shigeki S Hunter Mark S MS Batyuk Alexander A Oggenfuss Roland R Sander Mathias M Zerdane Serhane S Ozerov Dmitry D Nass Karol K Lemke Henrik H Mankowsky Roman R Brewster Aaron S AS Messinger Johannes J Sauter Nicholas K NK Yachandra Vittal K VK Yano Junko J Zouni Athina A Kern Jan J

Scientific reports 20211108 1

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 struct ...[more]

PMID: 34750381

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Project description:Room-temperature macromolecular crystallography allows protein structures to be determined under close-to-physiological conditions, permits dynamic freedom in protein motions and enables time-resolved studies. In the case of metalloenzymes that are highly sensitive to radiation damage, such room-temperature experiments can present challenges, including increased rates of X-ray reduction of metal centres and site-specific radiation-damage artefacts, as well as in devising appropriate sample-delivery and data-collection methods. It can also be problematic to compare structures measured using different crystal sizes and light sources. In this study, structures of a multifunctional globin, dehaloperoxidase B (DHP-B), obtained using several methods of room-temperature crystallographic structure determination are described and compared. Here, data were measured from large single crystals and multiple microcrystals using neutrons, X-ray free-electron laser pulses, monochromatic synchrotron radiation and polychromatic (Laue) radiation light sources. These approaches span a range of 18 orders of magnitude in measurement time per diffraction pattern and four orders of magnitude in crystal volume. The first room-temperature neutron structures of DHP-B are also presented, allowing the explicit identification of the hydrogen positions. The neutron data proved to be complementary to the serial femtosecond crystallography data, with both methods providing structures free of the effects of X-ray radiation damage when compared with standard cryo-crystallography. Comparison of these room-temperature methods demonstrated the large differences in sample requirements, data-collection time and the potential for radiation damage between them. With regard to the structure and function of DHP-B, despite the results being partly limited by differences in the underlying structures, new information was gained on the protonation states of active-site residues which may guide future studies of DHP-B.

Dataset Information

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

Publications

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

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