{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,4]],"date-time":"2026-04-04T05:21:12Z","timestamp":1775280072467,"version":"3.50.1"},"reference-count":25,"publisher":"Proceedings of the National Academy of Sciences","issue":"39","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2006,9,26]]},"abstract":"<jats:p>\n            The cobalt- and iron-containing corrinoid iron\u2013sulfur protein (CoFeSP) is functional in the acetyl-CoA (Ljungdahl\u2013Wood) pathway of autotrophic carbon fixation in various bacteria and archaea, where it is essential for the biosynthesis of acetyl-CoA. CoFeSP acts in two methylation reactions: the transfer of a methyl group from methyltransferase (MeTr)-bound methyltetrahydrofolate to the cob(I)amide of CoFeSP and the transfer of the methyl group of methyl-cob(III)amide to the reduced Ni-Ni-[4Fe-4S] active site cluster A of acetyl-CoA synthase (ACS). We have solved the crystal structure of as-isolated CoFeSP\n            <jats:sub>Ch<\/jats:sub>\n            from the CO-oxidizing hydrogenogenic bacterium\n            <jats:italic>Carboxydothermus hydrogenoformans<\/jats:italic>\n            at 1.9-\u00c5 resolution. The heterodimeric protein consists of two tightly interacting subunits with pseudo-twofold symmetry. The large CfsA subunit comprises three domains, of which the N-terminal domain binds the [4Fe-4S] cluster, the middle domain is a (\u03b2\u03b1)\n            <jats:sub>8<\/jats:sub>\n            -barrel, and the C-terminal domain shows an open fold and binds\n            <jats:italic>Co<\/jats:italic>\n            \u03b2-aqua-(5,6-dimethylbenzimidazolylcobamide) in a \u201cbase-off\u201d state without a protein ligand at the cobalt ion. The small CfsB subunit also displays a (\u03b2\u03b1)\n            <jats:sub>8<\/jats:sub>\n            -barrel fold and interacts with the upper side of the corrin macrocycle. Structure-based alignments show that both (\u03b2\u03b1)\n            <jats:sub>8<\/jats:sub>\n            -barrel domains are related to the MeTr in the acetyl-CoA pathway and to the folate domain of methionine synthase. We suggest that the C-terminal domain of the large subunit is the mobile element that allows the necessary interaction of CoFeSP\n            <jats:sub>Ch<\/jats:sub>\n            with the active site of ACS\n            <jats:sub>Ch<\/jats:sub>\n            and the methyltetrahydrofolate carrying MeTr. The conformation in the crystal structure shields the two open coordinations of cobalt and likely represents a resting state.\n          <\/jats:p>","DOI":"10.1073\/pnas.0601420103","type":"journal-article","created":{"date-parts":[[2006,9,19]],"date-time":"2006-09-19T00:57:41Z","timestamp":1158627461000},"page":"14331-14336","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":122,"title":["Structural insights into methyltransfer reactions of a corrinoid iron\u2013sulfur protein involved in acetyl-CoA synthesis"],"prefix":"10.1073","volume":"103","author":[{"given":"Tatiana","family":"Svetlitchnaia","sequence":"first","affiliation":[{"name":"*Laboratorium Proteinkristallographie,"}]},{"given":"Vitali","family":"Svetlitchnyi","sequence":"additional","affiliation":[{"name":"Lehrstuhl f\u00fcr Mikrobiologie, and"}]},{"given":"Ortwin","family":"Meyer","sequence":"additional","affiliation":[{"name":"Lehrstuhl f\u00fcr Mikrobiologie, and"},{"name":"Bayreuther Zentrum f\u00fcr Molekulare Biowissenschaften, Universit\u00e4t Bayreuth, 95440 Bayreuth, Germany"}]},{"given":"Holger","family":"Dobbek","sequence":"additional","affiliation":[{"name":"*Laboratorium Proteinkristallographie,"}]}],"member":"341","published-online":{"date-parts":[[2006,9,26]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.72.121801.161828"},{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr950058"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1075843"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)47238-3"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.178.2.340-346.1996"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0304262101"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183.17.5134-5144.2001"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)47936-7"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi9727996"},{"key":"e_1_3_4_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(00)00172-6"},{"key":"e_1_3_4_11_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.66.1.269"},{"key":"e_1_3_4_12_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1133218100"},{"key":"e_1_3_4_13_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1096-987X(199802)19:3<319::AID-JCC6>3.0.CO;2-W"},{"key":"e_1_3_4_14_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00888a030"},{"key":"e_1_3_4_15_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00449a019"},{"key":"e_1_3_4_16_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja054690o"},{"key":"e_1_3_4_17_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1489"},{"key":"e_1_3_4_18_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0308082100"},{"key":"e_1_3_4_19_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.7992050"},{"key":"e_1_3_4_20_2","doi-asserted-by":"publisher","DOI":"10.1038\/46972"},{"key":"e_1_3_4_21_2","first-page":"1","volume":"7","author":"La Fortelle E. d.","year":"1997","unstructured":"E. d. La Fortelle, JJ Irwin, G Bricogne Cryst Comp 7, 1\u20139 (1997).","journal-title":"Cryst Comp"},{"key":"e_1_3_4_22_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444994003112"},{"key":"e_1_3_4_24_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444998003254"},{"key":"e_1_3_4_25_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889892009944"},{"key":"e_1_3_4_26_2","unstructured":"WL DeLano PyMol.  (DeLano Scientific San Carlos CA 2002)."}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.0601420103","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,12]],"date-time":"2022-04-12T18:52:55Z","timestamp":1649789575000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.0601420103"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,9,26]]},"references-count":25,"journal-issue":{"issue":"39","published-print":{"date-parts":[[2006,9,26]]}},"alternative-id":["10.1073\/pnas.0601420103"],"URL":"https:\/\/doi.org\/10.1073\/pnas.0601420103","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2006,9,26]]},"assertion":[{"value":"2006-02-20","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2006-09-26","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}