{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T15:14:56Z","timestamp":1772118896179,"version":"3.50.1"},"reference-count":69,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2025,7,28]],"date-time":"2025-07-28T00:00:00Z","timestamp":1753660800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2026,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Amino acid L\u2010serine (L\u2010Ser) is a precursor of various biomolecules, including other amino acids, glutathione, and nucleotides. The metabolism of this amino acid is crucial in diseases such as brucellosis. Previous studies have revealed that the enzymes involved in L\u2010Ser biosynthesis are essential for\n                    <jats:italic>Brucella<\/jats:italic>\n                    replication, making them potential targets for the development of new drugs. Here, we focus on\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Brucella melitensis<\/jats:italic>\n                    <\/jats:styled-content>\n                    phosphoserine phosphatase (\n                    <jats:italic>Bm<\/jats:italic>\n                    PSP), which catalyzes the dephosphorylation of phosphoserine in L\u2010Ser. The enzyme is characterized through enzymatic and structural studies, leading to the discovery of its first crystallographic structures. The interactions of\n                    <jats:italic>Bm<\/jats:italic>\n                    PSP with different ligands are also investigated. We demonstrate that the substitution of its Mg\n                    <jats:sup>2+<\/jats:sup>\n                    cofactor with Ca\n                    <jats:sup>2+<\/jats:sup>\n                    inhibits the enzyme and results in a slight movement of catalytic residues in the active site. Crystallographic structures of\n                    <jats:italic>Bm<\/jats:italic>\n                    PSP in complex with substrate, reaction products, and substrate analogs are also detailed, revealing the interaction between these molecules and the active site residues. This structural study provides a better understanding of phosphoserine phosphatases, highlighting the involvement of two highly conserved residues in the mechanism of substrate entry into the active site.\n                  <\/jats:p>","DOI":"10.1002\/prot.70027","type":"journal-article","created":{"date-parts":[[2025,7,28]],"date-time":"2025-07-28T12:59:55Z","timestamp":1753707595000},"page":"502-514","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural and Enzymological Characterization of Phosphoserine Phosphatase From\n                    <i>Brucella melitensis<\/i>"],"prefix":"10.1002","volume":"94","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5762-4901","authenticated-orcid":false,"given":"Tanguy","family":"Scaillet","sequence":"first","affiliation":[{"name":"Department of Chemistry, Laboratoire de Chimie Biologique Structurale (CBS), University of Namur (UNamur) Namur Research Institute for Life Sciences (NARILIS), Namur Institute of Structural Matter (NISM)  Namur Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"\u00c9lise","family":"Pierson","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Laboratoire de Chimie Biologique Structurale (CBS), University of Namur (UNamur) Namur Research Institute for Life Sciences (NARILIS), Namur Institute of Structural Matter (NISM)  Namur Belgium"},{"name":"School of Biological Sciences, Victoria University of Wellington  Wellington New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marianne","family":"Fillet","sequence":"additional","affiliation":[{"name":"Laboratory for the Analysis of Medicines (LAM), Center for Interdisciplinary Research on Medicines (CIRM) University of Li\u00e8ge (ULi\u00e8ge)  Li\u00e8ge Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Johan","family":"Wouters","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Laboratoire de Chimie Biologique Structurale (CBS), University of Namur (UNamur) Namur Research Institute for Life Sciences (NARILIS), Namur Institute of Structural Matter (NISM)  Namur Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2025,7,28]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ymgme.2016.04.010"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj20021785"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrc3557"},{"key":"e_1_2_9_5_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00409-17"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(02)00324-8"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(00)00558-X"},{"key":"e_1_2_9_8_1","doi-asserted-by":"publisher","DOI":"10.1007\/s10969-011-9101-7"},{"key":"e_1_2_9_9_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.131213698"},{"key":"e_1_2_9_10_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.24238"},{"key":"e_1_2_9_11_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M311393200"},{"key":"e_1_2_9_12_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M112.449561"},{"key":"e_1_2_9_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2019.03.012"},{"issue":"6","key":"e_1_2_9_14_1","first-page":"592","article-title":"Crystal Structures and Snapshots Along the Reaction Pathway of Human Phosphoserine Phosphatase","volume":"75","author":"Haufroid M.","year":"2019","journal-title":"Acta Cryst"},{"key":"e_1_2_9_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejmech.2022.114935"},{"key":"e_1_2_9_16_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00840-19"},{"key":"e_1_2_9_17_1","doi-asserted-by":"publisher","DOI":"10.1021\/acsomega.3c09439"},{"key":"e_1_2_9_18_1","doi-asserted-by":"publisher","DOI":"10.3390\/ph12020066"},{"key":"e_1_2_9_19_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.biochem.7b01082"},{"key":"e_1_2_9_20_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-016-2177-2"},{"key":"e_1_2_9_21_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature10350"},{"key":"e_1_2_9_22_1","doi-asserted-by":"publisher","DOI":"10.1186\/s12876-021-02073-0"},{"key":"e_1_2_9_23_1","doi-asserted-by":"publisher","DOI":"10.21873\/anticanres.11574"},{"issue":"8","key":"e_1_2_9_24_1","first-page":"604","article-title":"Phosphoserine Phosphatase Promotes Lung Cancer Progression Through the Dephosphorylation of IRS\u20101 and a Noncanonical L\u2010Serine\u2010Independent Pathway","volume":"42","author":"Park S. 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