{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T19:46:05Z","timestamp":1791834365202,"version":"4.3.4"},"reference-count":65,"publisher":"National Academy of Sciences","issue":"42","license":[{"start":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T00:00:00Z","timestamp":1791763200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE-SC0016240 (DFS)"],"award-info":[{"award-number":["DE-SC0016240 (DFS)"]}],"id":[{"id":"10.13039\/100000015","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":[[2026,10,20]]},"abstract":"<jats:p>\n                    CO\n                    <jats:sub>2<\/jats:sub>\n                    transporters enable bacterial CO\n                    <jats:sub>2<\/jats:sub>\n                    -concentrating mechanisms by catalyzing directional hydration of CO\n                    <jats:sub>2<\/jats:sub>\n                    , yet the basis of this vectorial carbonic anhydrase (CA) activity remains an open question. We used cryoelectron microscopy to determine the structure of the DAB1 complex from\n                    <jats:italic toggle=\"yes\">Thermocrinis albus<\/jats:italic>\n                    to 2.29 \u00c5, revealing a heterotrimer in which a deeply buried \u03b2-CA active site in DabA is structurally coupled to the proton-translocating subunit DabB. Two conformational states define distinct solvent channels for substrate entry and product exit. A suppressor screen identifies mutations that disrupt coupling while retaining CA activity, underlying the importance of conserved residues that link proton translocation to active-site remodeling. These results support a model in which proton-driven conformational changes regulate substrate access to the active site, enabling vectorial CO\n                    <jats:sub>2<\/jats:sub>\n                    hydration.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2616712123","type":"journal-article","created":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T19:03:09Z","timestamp":1791831789000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Structural insights into the coupling mechanism of vectorial CO\n                    <sub>2<\/sub>\n                    uptake by DAB1"],"prefix":"10.1073","volume":"123","author":[{"given":"Naiya R.","family":"Phillips","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01an7q238","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Molecular and Cell Biology, University of California","place":["Berkeley"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5716-9980","authenticated-orcid":false,"given":"Luke M.","family":"Oltrogge","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01an7q238","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Molecular and Cell Biology, University of California","place":["Berkeley"]},{"id":[{"id":"https:\/\/ror.org\/01an7q238","id-type":"ROR","asserted-by":"publisher"}],"name":"HHMI, University of California","place":["Berkeley"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8317-4513","authenticated-orcid":false,"given":"Jonathan P.","family":"Remis","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01an7q238","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Physics, University of California","place":["Berkeley"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0042-2257","authenticated-orcid":false,"given":"David F.","family":"Savage","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01an7q238","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Molecular and Cell Biology, University of California","place":["Berkeley"]},{"id":[{"id":"https:\/\/ror.org\/01an7q238","id-type":"ROR","asserted-by":"publisher"}],"name":"HHMI, University of California","place":["Berkeley"]},{"id":[{"id":"https:\/\/ror.org\/01an7q238","id-type":"ROR","asserted-by":"publisher"}],"name":"Innovative Genomics Institute, University of California","place":["Berkeley"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2026,10,12]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"publisher","DOI":"10.3354\/ame01315"},{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1021\/acs.biochem.9b00237"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1111\/pce.12629"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/tpj.14674"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.arplant.50.1.539"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1093\/jxb\/erx110"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1007\/s11120-010-9608-y"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.00061-12"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0405211101"},{"key":"e_1_3_4_10_2","unstructured":"L. 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