{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T17:02:36Z","timestamp":1790701356748,"version":"4.1.0"},"reference-count":46,"publisher":"National Academy of Sciences","issue":"40","license":[{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000062","name":"HHS | NIH | National Institute of Diabetes and Digestive and Kidney Diseases","doi-asserted-by":"publisher","award":["DK122784"],"award-info":[{"award-number":["DK122784"]}],"id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM145416"],"award-info":[{"award-number":["GM145416"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,10,6]]},"abstract":"<jats:p>\n                    Mammalian phosphatidylserine synthase-1 and -2, PSS1 and PSS2, synthesize phosphatidylserine (PS) by replacing the headgroup of either phosphatidylcholine or phosphatidylethanolamine (PE) with a serine. We determined structures of PSS2 from\n                    <jats:italic toggle=\"yes\">Equus caballus<\/jats:italic>\n                    in complex with either a PE or a serine substrate to resolutions of 2.8 to 3.2 \u00c5. The structures define substrate binding sites and reveal that the phosphate group of the PE is coordinated by two Ca\n                    <jats:sup>2+<\/jats:sup>\n                    . In addition, we found that PSS2 has significant phospholipase D (PLD) activity in the absence of serine and that Ca\n                    <jats:sup>2+<\/jats:sup>\n                    is required for the PLD activity. These findings enrich and refine our knowledge in the mechanisms of substrate recognition and catalysis in mammalian PSS.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2607382123","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T16:18:26Z","timestamp":1790698706000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Mechanisms of substrate recognition and catalysis in a mammalian phosphatidylserine synthase 2"],"prefix":"10.1073","volume":"123","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9406-5168","authenticated-orcid":false,"given":"Lie","family":"Wang","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02pttbw34","id-type":"ROR","asserted-by":"publisher"}],"name":"Verna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of 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