{"entity": "researcher", "timestamp": "2026-08-22T06:57:27.915Z", "family": "Corbella", "given": "Marina", "initials": "M", "orcid": "0000-0001-9209-868X", "affiliations": ["Science for Life Laboratory, Department of Chemistry - BMC, Uppsala University, Box 576, S-751 23 Uppsala, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/53c414fb66534c3cbf91d3a3de055196.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/53c414fb66534c3cbf91d3a3de055196"}}, "publications": [{"entity": "publication", "iuid": "e3ac458a89954a7ab0a2ec3e5c8a6742", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/e3ac458a89954a7ab0a2ec3e5c8a6742.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/e3ac458a89954a7ab0a2ec3e5c8a6742"}}, "title": "Allosteric rescue of catalytically impaired ATP phosphoribosyltransferase variants links protein dynamics to active-site electrostatic preorganisation.", "authors": [{"family": "Fisher", "given": "Gemma", "initials": "G"}, {"family": "Corbella", "given": "Marina", "initials": "M", "orcid": "0000-0001-9209-868X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/53c414fb66534c3cbf91d3a3de055196.json"}}, {"family": "Alphey", "given": "Magnus S", "initials": "MS"}, {"family": "Nicholson", "given": "John", "initials": "J"}, {"family": "Read", "given": "Benjamin J", "initials": "BJ"}, {"family": "Kamerlin", "given": "Shina C L", "initials": "SCL", "orcid": "0000-0002-3190-1173", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c4540c85432f4cdf952b0ef7cfe1d875.json"}}, {"family": "da Silva", "given": "Rafael G", "initials": "RG", "orcid": "0000-0002-1308-8190", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/daa852e104244ccead6bf7a16a29790e.json"}}], "type": "journal article", "published": "2022-12-09", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "13", "issue": "1", "pages": "7607", "issn-l": "2041-1723"}, "abstract": "ATP phosphoribosyltransferase catalyses the first step of histidine biosynthesis and is controlled via a complex allosteric mechanism where the regulatory protein HisZ enhances catalysis by the catalytic protein HisGS while mediating allosteric inhibition by histidine. Activation by HisZ was proposed to position HisGS Arg56 to stabilise departure of the pyrophosphate leaving group. Here we report active-site mutants of HisGS with impaired reaction chemistry which can be allosterically restored by HisZ despite the HisZ:HisGS interface lying ~20 \u00c5 away from the active site. MD simulations indicate HisZ binding constrains the dynamics of HisGS to favour a preorganised active site where both Arg56 and Arg32 are poised to stabilise leaving-group departure in WT-HisGS. In the Arg56Ala-HisGS mutant, HisZ modulates Arg32 dynamics so that it can partially compensate for the absence of Arg56. These results illustrate how remote protein-protein interactions translate into catalytic resilience by restoring damaged electrostatic preorganisation at the active site.", "doi": "10.1038/s41467-022-34960-9", "pmid": "36494361", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC9734150"}, {"db": "pii", "key": "10.1038/s41467-022-34960-9"}], "notes": [], "created": "2026-08-21T11:49:18.662Z", "modified": "2026-08-21T11:49:18.775Z"}, {"entity": "publication", "iuid": "5b39a25a92404a84adf025ab9cb308b5", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/5b39a25a92404a84adf025ab9cb308b5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/5b39a25a92404a84adf025ab9cb308b5"}}, "title": "Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases.", "authors": [{"family": "Shen", "given": "Ruidan", "initials": "R"}, {"family": "Crean", "given": "Rory M", "initials": "RM"}, {"family": "Olsen", "given": "Keith J", "initials": "KJ"}, {"family": "Corbella", "given": "Marina", "initials": "M", "orcid": "0000-0001-9209-868X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/53c414fb66534c3cbf91d3a3de055196.json"}}, {"family": "Calixto", "given": "Ana R", "initials": "AR"}, {"family": "Richan", "given": "Teisha", "initials": "T"}, {"family": "Brand\u00e3o", "given": "Tiago A S", "initials": "TAS"}, {"family": "Berry", "given": "Ryan D", "initials": "RD"}, {"family": "Tolman", "given": "Alex", "initials": "A"}, {"family": "Loria", "given": "J Patrick", "initials": "JP"}, {"family": "Johnson", "given": "Sean J", "initials": "SJ", "orcid": "0000-0001-7992-2494", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4229ef82708c44c5bb6a3fabf913c44b.json"}}, {"family": "Kamerlin", "given": "Shina C L", "initials": "SCL", "orcid": "0000-0002-3190-1173", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c4540c85432f4cdf952b0ef7cfe1d875.json"}}, {"family": "Hengge", "given": "Alvan C", "initials": "AC", "orcid": "0000-0002-5696-2087", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/43fb9bec035e46c4a63263aded78a78b.json"}}], "type": "journal article", "published": "2022-11-23", "journal": {"title": "Chem Sci", "issn": "2041-6520", "volume": "13", "issue": "45", "pages": "13524-13540", "issn-l": null}, "abstract": "Protein tyrosine phosphatases (PTPs) possess a conserved mobile catalytic loop, the WPD-loop, which brings an aspartic acid into the active site where it acts as an acid/base catalyst. Prior experimental and computational studies, focused on the human enzyme PTP1B and the PTP from Yersinia pestis, YopH, suggested that loop conformational dynamics are important in regulating both catalysis and evolvability. We have generated a chimeric protein in which the WPD-loop of YopH is transposed into PTP1B, and eight chimeras that systematically restored the loop sequence back to native PTP1B. Of these, four chimeras were soluble and were subjected to detailed biochemical and structural characterization, and a computational analysis of their WPD-loop dynamics. The chimeras maintain backbone structural integrity, with somewhat slower rates than either wild-type parent, and show differences in the pH dependency of catalysis, and changes in the effect of Mg2+. The chimeric proteins' WPD-loops differ significantly in their relative stability and rigidity. The time required for interconversion, coupled with electrostatic effects revealed by simulations, likely accounts for the activity differences between chimeras, and relative to the native enzymes. Our results further the understanding of connections between enzyme activity and the dynamics of catalytically important groups, particularly the effects of non-catalytic residues on key conformational equilibria.", "doi": "10.1039/d2sc04135a", "pmid": "36507179", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC9682893"}, {"db": "pii", "key": "d2sc04135a"}], "notes": [], "created": "2026-08-21T11:58:06.696Z", "modified": "2026-08-21T11:58:06.822Z"}, {"entity": "publication", "iuid": "519b285dd47440b999323898a773c73b", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/519b285dd47440b999323898a773c73b.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/519b285dd47440b999323898a773c73b"}}, "title": "Correction to \"Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases\".", "authors": [{"family": "Crean", "given": "Rory M", "initials": "RM"}, {"family": "Biler", "given": "Michal", "initials": "M", "orcid": "0000-0003-3809-6928", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c4e9f22f57e441cb9028720d6a4b2bfa.json"}}, {"family": "Corbella", "given": "Marina", "initials": "M", "orcid": "0000-0001-9209-868X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/53c414fb66534c3cbf91d3a3de055196.json"}}, {"family": "Calixto", "given": "Ana R", "initials": "AR", "orcid": "0000-0002-1123-0413", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/91f7bbeb7f3245449679931f97d21eb8.json"}}, {"family": "van der Kamp", "given": "Marc W", "initials": "MW", "orcid": "0000-0002-8060-3359", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9e09f39776374aeca06c0a767d62bfac.json"}}, {"family": "Hengge", "given": "Alvan C", "initials": "AC", "orcid": "0000-0002-5696-2087", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/43fb9bec035e46c4a63263aded78a78b.json"}}, {"family": "Kamerlin", "given": "Shina C L", "initials": "SCL", "orcid": "0000-0002-3190-1173", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c4540c85432f4cdf952b0ef7cfe1d875.json"}}], "type": "published erratum", "published": "2022-06-08", "journal": {"title": "Journal of the American Chemical Society", "issn": "1520-5126", "volume": "144", "issue": "22", "pages": "10091-10093", "issn-l": "0002-7863"}, "abstract": null, "doi": "10.1021/jacs.2c04624", "pmid": "35609280", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11027752"}], "notes": [], "created": "2026-08-21T11:37:56.469Z", "modified": "2026-08-21T11:37:56.639Z"}]}