{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T14:47:34Z","timestamp":1785422854567,"version":"3.56.0"},"reference-count":45,"publisher":"International Union of Crystallography (IUCr)","issue":"10","license":[{"start":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T00:00:00Z","timestamp":1757635200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T00:00:00Z","timestamp":1757635200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"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":[[2025,9,4]]},"published-print":{"date-parts":[[2025,10,1]]},"abstract":"<jats:p>\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    DegQ is a 46-amino-acid regulatory protein involved in the DegS\u2013DegU two-component system. DegQ promotes the phosphorylation of DegU by DegS, switching the function of DegU from competence to the induction of poly-\u03b3-glutamate production. To elucidate its structural role, we determined the crystal structures of wild-type DegQ and its mutant DegQS25L. Each DegQ monomer folds into a single \u03b1-helix, and four monomers assemble into a tetramer characterized by a four-helix coiled-coil structure. Within the tetramer, two adjacent helices are oriented in the same direction, while the other two are oriented oppositely, forming a pseudo-twofold symmetric arrangement. The mutant form displays disrupted symmetry due to altered helix packing, which is caused by shifts in the coiled-coil heptad register induced by the mutation. Structural predictions using\n                    <jats:italic>AlphaFold<\/jats:italic>\n                    3 suggest that DegQ likely binds to the N-terminal helix bundle of DegS, either as a dimer or as individual monomers. These findings provide structural insight into DegQ oligomerization and its potential role in modulating DegS autophosphorylation and DegU binding.\n                  <\/jats:p>","DOI":"10.1107\/s2053230x25007903","type":"journal-article","created":{"date-parts":[[2025,9,10]],"date-time":"2025-09-10T13:38:26Z","timestamp":1757511506000},"page":"425-433","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":1,"title":["Tetrameric structure of\n                    <i>Bacillus subtilis<\/i>\n                    DegQ and its predicted interaction with the DegS\u2013DegU two-component system"],"prefix":"10.1107","volume":"81","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3551-6854","authenticated-orcid":true,"given":"Zui","family":"Fujimoto","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/023v4bd62","id-type":"ROR","asserted-by":"publisher"}],"department":["Research Center for Advanced Analysis"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-9758-0052","authenticated-orcid":true,"given":"Naomi","family":"Kishine","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/023v4bd62","id-type":"ROR","asserted-by":"publisher"}],"department":["Research Center for Advanced Analysis"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kengo","family":"Saitou","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/023v4bd62","id-type":"ROR","asserted-by":"publisher"}],"department":["Institute of Food Research"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4641-4041","authenticated-orcid":true,"given":"Keitarou","family":"Kimura","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/023v4bd62","id-type":"ROR","asserted-by":"publisher"}],"department":["Institute of Food Research"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2025,9,12]]},"reference":[{"key":"bus5004_bb1","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"bus5004_bb2","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1128\/jb.169.1.324-333.1987","volume":"169","author":"Amory","year":"1987","journal-title":"J. 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