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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,9,8]]},"abstract":"<jats:p>\n                    Maturation of urease, a virulence factor for\n                    <jats:italic toggle=\"yes\">Helicobacter pylori<\/jats:italic>\n                    infection, requires the delivery of nickel ions to the metalloenzyme. To avoid cytotoxicity, Ni(II) ions are transferred within protein complexes of metallochaperones to ensure that the toxic metal does not escape into the cytoplasm. In the urease maturation pathway, metallochaperone UreG receives its Ni(II) ions by forming a 2:2 complex with another metallochaperone UreE. Using C-terminal truncation variants of UreE [UreE(1-158) and UreE(1-148)], we determined the crystal structures of the UreE\n                    <jats:sub>2<\/jats:sub>\n                    G\n                    <jats:sub>2<\/jats:sub>\n                    complex bound with Ni(II) ions and GMPPNP, a nonhydrolyzable GTP analogue. UreE\u2013UreG interactions are asymmetric, with the UreG dimer interacting mainly with the proximal UreE (closest to UreG). GTP binding induces conformational changes in the residues Asp37-Asp43 and the CPH motif (Cys66-Pro67-His68) of distal UreG that enable its anchorage to the UreE\n                    <jats:sub>2<\/jats:sub>\n                    G\n                    <jats:sub>2<\/jats:sub>\n                    complex. His68 of distal UreG moves toward and chelates a Ni(II) ion at the UreE binding site. Formation of the UreE\n                    <jats:sub>2<\/jats:sub>\n                    G\n                    <jats:sub>2<\/jats:sub>\n                    complex juxtaposes the Ni(II) binding sites of UreE and UreG. Supported by in vitro binding analyses, structural comparison suggests that nickel transfer from UreE to UreG induces conformational changes that weaken UreE\u2013UreG interactions, thereby providing a mechanism for the dissociation of Ni(II)-bound UreG from the UreE\n                    <jats:sub>2<\/jats:sub>\n                    G\n                    <jats:sub>2<\/jats:sub>\n                    complex. Our work presents a paradigm on how GTP and Ni(II) binding allosterically regulate the formation of a metallochaperone complex to facilitate nickel transfer.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2535662123","type":"journal-article","created":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T17:36:55Z","timestamp":1788457015000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Structural insights into how metallochaperones UreE and UreG interact to deliver a toxic metal to urease"],"prefix":"10.1073","volume":"123","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-1577-3118","authenticated-orcid":false,"given":"Chun-Long","family":"Chan","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00t33hh48","id-type":"ROR","asserted-by":"publisher"}],"name":"School of Life Sciences, Centre for Protein Science and Crystallography, State Key Laboratory of Agrobiotechnology, The Chinese University of 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LLC The PyMOL molecular graphics system (Version 3.0 NY 2025)."},{"key":"e_1_3_4_53_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac60252a045"},{"key":"e_1_3_4_54_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)38872-6"},{"key":"e_1_3_4_55_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.58.4.992-998.1990"},{"key":"e_1_3_4_56_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1008398227519"},{"key":"e_1_3_4_57_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja982649y"},{"key":"e_1_3_4_58_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1008268930690"},{"key":"e_1_3_4_59_2","first-page":"1137","article-title":"Double spin-state-selective coherence transfer. Application for two-dimensional selection of multiplet components with long transverse relaxation times","volume":"96","author":"Meissner A.","year":"1998","unstructured":"A. Meissner, T. Schulte-Herbruggen, J. Briand, O. W. Sorensen, Double spin-state-selective coherence transfer. Application for two-dimensional selection of multiplet components with long transverse relaxation times. Mol. Phys. 96, 1137\u20131142 (1998).","journal-title":"Mol. Phys."},{"key":"e_1_3_4_60_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmre.1998.1483"},{"key":"e_1_3_4_61_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00197809"},{"key":"e_1_3_4_62_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00404272"},{"key":"e_1_3_4_63_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkn322"},{"key":"e_1_3_4_64_2","unstructured":"C. L. Chan K. B. Wong Crystal Structure of Helicobacter pylori Urease Accessory Protein UreE(1-158) and UreG in complex with GMPPNP and nickel. Protein Data Bank. https:\/\/www.rcsb.org\/structure\/20ZY. Deposited 4 December 2025."},{"key":"e_1_3_4_65_2","unstructured":"C. L. Chan K. B. Wong Crystal Structure of Helicobacter pylori Urease Accessory Protein UreE(1-148) and UreG in complex with GMPPNP and nickel. Protein Data Bank. https:\/\/www.rcsb.org\/structure\/21AD. Deposited 4 December 2025."}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.2535662123","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T17:37:11Z","timestamp":1788457031000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/10.1073\/pnas.2535662123"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,3]]},"references-count":65,"journal-issue":{"issue":"36","published-print":{"date-parts":[[2026,9,8]]}},"alternative-id":["10.1073\/pnas.2535662123"],"URL":"https:\/\/doi.org\/10.1073\/pnas.2535662123","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,3]]},"assertion":[{"value":"2025-12-14","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-08-06","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-09-03","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"e2535662123"}}