{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["de Jong NWM"],"funding":["ZonMw (Netherlands Organization for Health Research and Development)","BLRD VA","NIAID NIH HHS","ZonMw","HHS NIH National Institute of General Medical Sciences (NIGMS)","HHS NIH National Institute of Allergy and Infectious Diseases (NIAID)","NIGMS NIH HHS"],"pagination":["2260-2271"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5818189"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["293(7)"],"pubmed_abstract":["The heme-containing enzyme myeloperoxidase (MPO) is critical for optimal antimicrobial activity of human neutrophils. We recently discovered that the bacterium <i>Staphylococcus aureus</i> expresses a novel immune evasion protein, called SPIN, that binds tightly to MPO, inhibits MPO activity, and contributes to bacterial survival following phagocytosis. A co-crystal structure of SPIN bound to MPO suggested that SPIN blocks substrate access to the catalytic heme by inserting an N-terminal β-hairpin into the MPO active-site channel. Here, we describe a series of experiments that more completely define the structure/function relationships of SPIN. Whereas the SPIN N terminus adopts a β-hairpin confirmation upon binding to MPO, the solution NMR studies presented here are consistent with this r"],"journal":["The Journal of biological chemistry"],"pubmed_title":["A structurally dynamic N-terminal region drives function of the staphylococcal peroxidase inhibitor (SPIN)."],"pmcid":["PMC5818189"],"funding_grant_id":["GM121511","R21 AI111203","205200004","AI116546","R01 GM121511","AI111203","R01 AI116546","I01 BX000513"],"pubmed_authors":["Garcia BL","Katz BB","Herrera AI","Prakash O","van Strijp JAG","Geisbrecht BV","van Kessel KPM","de Jong NWM","Ramyar KX","Ploscariu NT","Nauseef WM","Leidal KG"],"additional_accession":[]},"is_claimable":false,"name":"A structurally dynamic N-terminal region drives function of the staphylococcal peroxidase inhibitor (SPIN).","description":"The heme-containing enzyme myeloperoxidase (MPO) is critical for optimal antimicrobial activity of human neutrophils. We recently discovered that the bacterium <i>Staphylococcus aureus</i> expresses a novel immune evasion protein, called SPIN, that binds tightly to MPO, inhibits MPO activity, and contributes to bacterial survival following phagocytosis. A co-crystal structure of SPIN bound to MPO suggested that SPIN blocks substrate access to the catalytic heme by inserting an N-terminal β-hairpin into the MPO active-site channel. Here, we describe a series of experiments that more completely define the structure/function relationships of SPIN. Whereas the SPIN N terminus adopts a β-hairpin confirmation upon binding to MPO, the solution NMR studies presented here are consistent with this r","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Feb","modification":"2026-04-30T20:24:39.965Z","creation":"2019-03-26T22:54:58Z"},"accession":"S-EPMC5818189","cross_references":{"pubmed":["29306874"],"doi":["10.1074/jbc.ra117.000134","10.1074/jbc.RA117.000134"]}}