{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,8]],"date-time":"2026-06-08T10:20:36Z","timestamp":1780914036469,"version":"3.54.1"},"reference-count":45,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T00:00:00Z","timestamp":1772236800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T00:00:00Z","timestamp":1772236800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","award":["GAP0384"],"award-info":[{"award-number":["GAP0384"]}],"id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001412","name":"Council of Scientific and Industrial Research, India","doi-asserted-by":"publisher","award":["MLP007"],"award-info":[{"award-number":["MLP007"]}],"id":[{"id":"10.13039\/501100001412","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2026,6]]},"abstract":"<jats:p>\n                    The ESX\u20105 secretion system in\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    exports PE\/PPE virulence factors, with EccA5, an AAA+ ATPase, playing a pivotal role. We solved the crystal structure of EccA5's N\u2010terminal TPR domain (EccA5NT) at 2.15\u2009\u00c5, revealing a monomeric fold with six TPR motifs and a variable \u03b2\u2010finger. Biophysical studies, including SAXS and size exclusion chromatography, confirm its monomeric state. A flexible loop (residues 137\u2013148) suggests dynamic substrate interactions. SPR, SAXS and\n                    <jats:italic>in silico<\/jats:italic>\n                    docking show moderate binding (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>D<\/jats:sub>\n                    \u2009=\u20093.43\u2009\u03bc\n                    <jats:sc>m<\/jats:sc>\n                    ) between EccA5NT's \u03b2\u2010finger and EspG5's \u03b22\u2010\u03b23 loop, indicating a role in PE\/PPE\u2010EspG5 complex disassembly. These findings elucidate the role of EccA5 in ESX\u20105\u2010mediated secretion.\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.70315","type":"journal-article","created":{"date-parts":[[2026,3,8]],"date-time":"2026-03-08T23:33:27Z","timestamp":1773012807000},"page":"1605-1620","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The crystal structure of the\n                    <scp>TPR<\/scp>\n                    domain of the\n                    <scp>EccA5 ATPase<\/scp>\n                    and demonstration of its interaction with\n                    <scp>EspG5<\/scp>\n                    from the mycobacterial\n                    <scp>ESX<\/scp>\n                    \u20105 pathway"],"prefix":"10.1002","volume":"600","author":[{"given":"Vijay Kumar","family":"Sharma","sequence":"first","affiliation":[{"name":"Biochemistry and Structural Biology Division CSIR\u2010Central Drug Research Institute  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