{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:13:22Z","timestamp":1792786402541,"version":"4.5.0"},"reference-count":21,"publisher":"International Union of Crystallography (IUCr)","issue":"10","license":[{"start":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T00:00:00Z","timestamp":1789603200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"},{"start":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T00:00:00Z","timestamp":1789603200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"}],"funder":[{"name":"Woosuk University","id":[{"id":"https:\/\/ror.org\/00emz0366","id-type":"ROR","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100002701","name":"Ministry of Education","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002701","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Jeonbuk State"},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2026-25598245"],"award-info":[{"award-number":["RS-2026-25598245"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"accepted":{"date-parts":[[2026,8,31]]},"published-print":{"date-parts":[[2026,10,1]]},"abstract":"<jats:p>\n                    The catalytic domain of\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    dihydrolipoamide succinyltransferase (\n                    <jats:italic>Ec<\/jats:italic>\n                    DSCD), the E2 component of the 2-oxoglutarate dehydrogenase complex, forms the oligomeric core of the multi-enzyme assembly. Here, we report the crystal structure of\n                    <jats:italic>Ec<\/jats:italic>\n                    DSCD determined in space group\n                    <jats:italic>F<\/jats:italic>\n                    432. The\n                    <jats:italic>F<\/jats:italic>\n                    432 crystal symmetry captures a compact trimeric building block and a symmetry-expanded 24-subunit assembly consistent with the octahedral architecture of the E2 catalytic core. Structural analysis revealed sulfate-compatible electron density near Lys196 at a crystallographic threefold intratrimeric junction. Comparison with previously reported\n                    <jats:italic>Ec<\/jats:italic>\n                    DSCD structures suggests that this density marks a structurally relevant oxyanion-sensitive hotspot at the intratrimeric junction. Notably, the \u03b11-helix is positioned adjacent to the Lys196-centered junction and extends towards the active-site pocket, where it adopts a shifted orientation relative to other\n                    <jats:italic>Ec<\/jats:italic>\n                    DSCD crystal forms. These observations link sulfate-compatible density, the intratrimeric junction and \u03b11-helix positioning within the\n                    <jats:italic>Ec<\/jats:italic>\n                    DSCD 24-mer, providing a structural framework for understanding local oxyanion-sensitive features in the E2 catalytic core.\n                  <\/jats:p>","DOI":"10.1107\/s2053230x2600909x","type":"journal-article","created":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T15:10:46Z","timestamp":1789485046000},"page":"362-368","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":0,"title":["Sulfate-compatible density marks an intratrimeric junction in the\n                    <i>Escherichia coli<\/i>\n                    dihydrolipoamide succinyltransferase catalytic domain"],"prefix":"10.1107","volume":"82","author":[{"given":"Bison","family":"Lim","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00emz0366","id-type":"ROR","asserted-by":"publisher"}],"department":["College of Pharmacy"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eunji","family":"Kim","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00emz0366","id-type":"ROR","asserted-by":"publisher"}],"department":["College of Pharmacy"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jungeun","family":"Byun","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00emz0366","id-type":"ROR","asserted-by":"publisher"}],"department":["College of Pharmacy"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-2415-6580","authenticated-orcid":true,"given":"Minjeong","family":"Kim","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00emz0366","id-type":"ROR","asserted-by":"publisher"}],"department":["College of Pharmacy"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5214-3036","authenticated-orcid":true,"given":"Hyo Jung","family":"Kim","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00emz0366","id-type":"ROR","asserted-by":"publisher"}],"department":["College of Pharmacy"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2026,9,17]]},"reference":[{"key":"ft5129_bb1","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Cryst. 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