{"id":55755,"date":"2025-12-15T15:11:24","date_gmt":"2025-12-15T15:11:24","guid":{"rendered":"https:\/\/matis.is\/new-matis-is\/?p=55755"},"modified":"2025-12-15T15:11:25","modified_gmt":"2025-12-15T15:11:25","slug":"crystal-structure-enzymatic-and-thermodynamic-properties-of-the-thermus-thermophilus-phage-tt72-lytic-endopeptidase-with-unique-structural-signatures-of-thermal-adaptation","status":"publish","type":"post","link":"https:\/\/matis.is\/en\/greinar\/crystal-structure-enzymatic-and-thermodynamic-properties-of-the-thermus-thermophilus-phage-tt72-lytic-endopeptidase-with-unique-structural-signatures-of-thermal-adaptation\/","title":{"rendered":"Crystal structure, enzymatic and thermodynamic properties of the\u00a0Thermus thermophilus\u00a0phage Tt72 lytic endopeptidase with unique structural signatures of thermal adaptation"},"content":{"rendered":"<p>We presents the discovery and molecular characterization of a novel lytic enzyme from the extremophilic\u00a0<em>Thermus thermophilus<\/em>\u00a0MAT72 phage vB_Tt72. The protein of 346-aa (MW\u00a0=\u00a039,705) functions as phage vB_Tt72 endolysin and shows low sequence identity (&lt;37\u00a0%) to members of M23 family of peptidoglycan hydrolases, except for two uncharacterized endopeptidases of\u00a0<em>T. thermophilus<\/em>\u00a0phages: \u03c6YS40 (87\u00a0%) and \u03c6TMA (88\u00a0%). The enzyme exhibits lytic activity mainly against bacteria of the genus\u00a0<em>Thermus<\/em>and, to a lesser extent, against other Gram-negative and Gram-positive bacteria. The protein is monomeric in solution and is highly thermostable (T<sub>m<\/sub>\u00a0=\u00a098.3\u00a0\u00b0C). It retains\u00a0\u223c\u00a050\u00a0% of its lytic activity after 90\u00a0min of incubation at 99\u00a0\u00b0C. Crystallographic analysis, at 2.2\u00a0\u00c5 resolution, revealed a fold characteristic of M23 metallopeptidases, accounting for 40\u00a0% of the structure. The remaining parts of the molecule are folded in a manner that was previously undescribed. The M23 fold contains a Zn<sup>2+<\/sup>\u00a0ion coordinated by a conserved His-Asp-His triad, and two conserved His residues essential for catalysis. The active site is occupied by a phosphate or a sulfate anion, while the substrate-binding groove contains a ligand, which is a fragment of\u00a0<em>E. coli<\/em>\u00a0peptidoglycan. The common sequence-based criteria failed to identify the protein as (hyper)thermophilic. It is likely that the protein\u2019s thermal stability is owed to peculiar features of its three-dimensional structure. Instead of trimmed surface loops, observed in many thermostable proteins, the catalytic domain contains two long loops that interlace and form an \u03b1-helical bundle with its own hydrophobic core.<\/p>","protected":false},"excerpt":{"rendered":"<p>We presents the discovery and molecular characterization of a novel lytic enzyme from the extremophilic\u00a0Thermus thermophilus\u00a0MAT72 phage vB_Tt72. The protein [&hellip;]<\/p>\n","protected":false},"author":7,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"_uag_custom_page_level_css":"","site-sidebar-layout":"default","site-content-layout":"","ast-site-content-layout":"default","site-content-style":"default","site-sidebar-style":"default","ast-global-header-display":"","ast-banner-title-visibility":"","ast-main-header-display":"","ast-hfb-above-header-display":"","ast-hfb-below-header-display":"","ast-hfb-mobile-header-display":"","site-post-title":"","ast-breadcrumbs-content":"","ast-featured-img":"","footer-sml-layout":"","ast-disable-related-posts":"","theme-transparent-header-meta":"","adv-header-id-meta":"","stick-header-meta":"","header-above-stick-meta":"","header-main-stick-meta":"","header-below-stick-meta":"","astra-migrate-meta-layouts":"default","ast-page-background-enabled":"default","ast-page-background-meta":{"desktop":{"background-color":"var(--ast-global-color-5)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"ast-content-background-meta":{"desktop":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"footnotes":""},"categories":[2011],"tags":[2540,2544,2541,2545,2543],"class_list":["post-55755","post","type-post","status-publish","format-standard","hentry","category-greinar","tag-bacteriophage","tag-crystal-structure","tag-endolysin","tag-m23-domain","tag-thermostable-lytic-protein"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.2 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Crystal structure, enzymatic and thermodynamic properties of the\u00a0Thermus thermophilus\u00a0phage Tt72 lytic endopeptidase with unique structural signatures of thermal adaptation - Mat\u00eds<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/matis.is\/en\/greinar\/crystal-structure-enzymatic-and-thermodynamic-properties-of-the-thermus-thermophilus-phage-tt72-lytic-endopeptidase-with-unique-structural-signatures-of-thermal-adaptation\/\" \/>\n<meta property=\"og:locale\" content=\"en_GB\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Crystal structure, enzymatic and thermodynamic properties of the\u00a0Thermus thermophilus\u00a0phage Tt72 lytic endopeptidase with unique structural signatures of thermal adaptation - Mat\u00eds\" \/>\n<meta property=\"og:description\" content=\"We presents the discovery and molecular characterization of a novel lytic enzyme from the extremophilic\u00a0Thermus thermophilus\u00a0MAT72 phage vB_Tt72. 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