Comparison of water networks in plant and cyanobacterial photosystem II based on a 2.44 Å resolution structure from Arabidopsis thaliana

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Comparison of water networks in plant and cyanobacterial photosystem II based on a 2.44 Å resolution structure from Arabidopsis thaliana | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Comparison of water networks in plant and cyanobacterial photosystem II based on a 2.44 Å resolution structure from Arabidopsis thaliana Johannes Messinger, Jack Forsman, André Graça, Abuzer Aydin, Michael Hall, and 2 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-6604913/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract Photosystem II (PS II) is a large membrane-bound protein complex that catalyzes light-driven water oxidation in plants and cyanobacteria. Here, we present the first high-resolution structure of an intact and active PS II from Arabidopsis thaliana at 2.44 Å resolution, which to date represents the highest resolution structure of PS II from higher plants. At this improved resolution we are able to identify many water molecules within the PS II structure, including waters around the water-splitting manganese cluster, the non-heme iron, and within the water/proton channels connecting these active sites to the protein exterior. By comparing this new Arabidopsis thaliana structure to the highest resolution PS II structure from cyanobacteria, we identified conserved features which are likely to be essential in the water networks of plants and cyanobacteria. Our findings further the understanding of the importance and design principles of protein-water-cofactor interactions in photosynthetic water splitting and quinone reduction in photosystem II. Biological sciences/Structural biology/Electron microscopy/Cryoelectron microscopy Biological sciences/Plant sciences/Photosynthesis/Photosystem II Biological sciences/Biochemistry/Enzyme mechanisms Full Text Additional Declarations There is NO Competing Interest. Supplementary Files ArabiSupplementalv5.docx Supplementary Material for NCOMMS-25-33937 Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. 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