{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T09:14:11Z","timestamp":1789550051075,"version":"build-2803163510"},"reference-count":47,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T00:00:00Z","timestamp":1782950400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:p>\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    (\n                    <jats:italic>Mtb<\/jats:italic>\n                    ) phosphoserine phosphatase SerB2 is a key enzyme essential for bacterial survival and virulence, catalyzing the final step in the L-serine biosynthesis pathway. SerB2 is an attractive drug target due to its role in immune evasion by\n                    <jats:italic>Mtb<\/jats:italic>\n                    . However, the functional mechanism of\n                    <jats:italic>Mtb<\/jats:italic>\n                    SerB2 remains poorly understood. Here, we measured the hydrodynamic radius of monomeric SerB2 to be 5.4 \u00b1 0.3 nm. Based on an AlphaFold2-predicted structural model, molecular docking was performed and site-specific mutations were carried out. Mutants D185A, D187A, E194A, S226A, R230A or K318A exhibited significantly reduced activity. In contrast, deletion of segment 294\u2013314 (\u0394294\u2013314) increased activity. Notably, the 294\u2013314 region exhibited higher flexibility compared to other parts of SerB2. Among the inhibitors tested, clofazimine displayed the most potent inhibitory effect. Our findings offer new insights into the mechanisms of SerB2 function and lay the structural and biochemical groundwork for developing novel anti-tuberculosis therapies.\n                  <\/jats:p>","DOI":"10.3389\/fmicb.2026.1863671","type":"journal-article","created":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T05:35:45Z","timestamp":1782970545000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":3,"title":["Molecular insights into the functional mechanism of phosphoserine phosphatase SerB2 in Mycobacterium tuberculosis"],"prefix":"10.3389","volume":"17","author":[{"given":"Dafeng","family":"Liu","sequence":"first","affiliation":[{"name":"Key Laboratory of Microbial Resources Protection, Development and Utilization, College of Biological Sciences and Technology, Yili Normal University, Yining","place":["Xinjiang, China"]},{"name":"School of Life Sciences, Xiamen University, Xiamen","place":["Fujian, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huashui","family":"Deng","sequence":"additional","affiliation":[{"name":"School of Life Sciences, Xiamen University, Xiamen","place":["Fujian, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinbao","family":"Liu","sequence":"additional","affiliation":[{"name":"School of Life Sciences, Xiamen University, Xiamen","place":["Fujian, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenshuang","family":"Yao","sequence":"additional","affiliation":[{"name":"School of Life Sciences, Xiamen University, Xiamen","place":["Fujian, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Na","family":"Li","sequence":"additional","affiliation":[{"name":"Key Laboratory of Microbial Resources Protection, Development and Utilization, College of Biological Sciences and Technology, Yili Normal University, Yining","place":["Xinjiang, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,7,2]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers.","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"B2","doi-asserted-by":"publisher","first-page":"25149","DOI":"10.1074\/jbc.M114.597682","article-title":"High throughput screen identifies small molecule inhibitors specific for Mycobacterium tuberculosis phosphoserine phosphatase.","volume":"289","author":"Arora","year":"2014","journal-title":"J. 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