{"id":25694,"date":"2011-02-14T21:00:00","date_gmt":"2011-02-14T20:00:00","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=25694"},"modified":"2024-11-14T16:30:27","modified_gmt":"2024-11-14T15:30:27","slug":"two-in-one","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/two-in-one\/","title":{"rendered":"Two in one"},"content":{"rendered":"\n<div class=\"wp-block-image\"><figure class=\"vf-figure  | vf-figure--align vf-figure--align-inline-start   size-medium\"><a href=\"http:\/\/medias01-web.embl.de\/Mediasite\/Play\/14c349f4a7474668bd89ea42f17d378b1d\" target=\"_blank\" rel=\"noopener noreferrer\"><img loading=\"lazy\" decoding=\"async\" width=\"300\" height=\"180\" class=\"vf-figure__image\" src=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2011\/02\/PriA-300x180.jpg\" alt=\"3D structure of Mycobacterium tuberculosis\u2019 enzyme PriA\" class=\"wp-image-25704\" srcset=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2011\/02\/PriA-300x180.jpg 300w, https:\/\/www.embl.org\/news\/wp-content\/uploads\/2011\/02\/PriA-768x461.jpg 768w, https:\/\/www.embl.org\/news\/wp-content\/uploads\/2011\/02\/PriA.jpg 1000w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a><figcaption class=\"vf-figure__caption\">Three snapshots of the 3D structure of Mycobacterium tuberculosis\u2019 enzyme PriA are combined in this video to show the changes the enzyme is capable of undergoing.\n\nClick to play. Video credits: EMBL\/Felix List.<\/figcaption><\/figure><\/div>\n\n\n\n<p>In a paper published online today in <em>PNAS<\/em>, scientists from the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, reveal new insights into the workings of enzymes from a group of bacteria including <em>Mycobacterium tuberculosis<\/em>, the bacterium that causes tuberculosis. The new findings present possible new opportunities for developing organism-specific drugs, which target the pathogen but leave other microorganisms, which are beneficial to us, untouched.<\/p>\n\n\n\n<p>Tuberculosis remains one of the largest threats to human health worldwide, and one of the most frequent causes of death in HIV patients. With the increasing emergence of strains of <em>Mycobacterium tuberculosis<\/em> that are hyper-resistant to drugs, it becomes ever more urgent that novel treatments be developed, and the search for novel strategies for drug development is an important step in this process.<\/p>\n\n\n\n<p>In the current study, <a href=\"http:\/\/www.embl.org\/groups\/wilmanns\/\">Matthias Wilmanns and his\u00a0group at EMBL<\/a> identified a multi-tasking enzyme from <em>Mycobacterium tuberculosis<\/em> that catalyses reactions on two different molecules, or substrates. In most organisms, cells need two specific enzymes, known as HisA and TrpF, in order to produce two essential amino acids \u2013 histidine and tryptophan. However, in <em>Mycobacterium tuberculosis<\/em>, the encoding gene for TrpF is missing, and the two reactions are instead catalysed by a single enzyme, which is able to recognize and bind to two different substrates. This enzyme is known as PriA.<\/p>\n\n\n\n<p>Using the <em>Mycobacterium tuberculosis<\/em> version of the PriA enzyme as a model, the researchers were able to unravel the hitherto unknown mechanism of bi-substrate specific binding observed in this group of bacteria.<\/p>\n\n\n\n<p>\u201cWhen we solved the three-dimensional structure of PriA, we found that it has the unique ability to form two different substrate-specific active sites,\u201d Wilmanns says: \u201cit can form a reaction-specific active site, or undergo what we call \u2018substrate-induced metamorphosis\u2019 to form a different active site.\u201d<\/p>\n\n\n\n<p>To further verify these observations, Wilmanns and colleagues screened 20,000 small molecule compounds, and identified a handful which inhibited both PriA-catalysed reactions but had no effect on TrpF activity.<\/p>\n\n\n\n<p>\u201cWe believe that this ability for bi-substrate catalysis in <em>Mycobacterium tuberculosis<\/em> could be a new opportunity for future drug development,\u201d Wilmanns concludes: \u201cThis organism-specific reaction process could be exploited, since only the pathogen but none of the other bacteria living in or on humans, many of which are important for our well being, would be targeted.\u201d<\/p>\n","protected":false},"excerpt":{"rendered":"<p>In a paper published online today in PNAS, scientists from the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, reveal new insights into the workings of enzymes from a group of bacteria including Mycobacterium tuberculosis, the bacterium that causes tuberculosis. The new findings&hellip;<\/p>\n","protected":false},"author":16,"featured_media":25704,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[266,53,1748,764,306],"embl_taxonomy":[9596,19039,19403],"class_list":["post-25694","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-enzyme","tag-hamburg","tag-press-release","tag-tuberculosis","tag-wilmanns","embl_taxonomy-embl-hamburg","embl_taxonomy-matthias-wilmanns","embl_taxonomy-wilmanns-group"],"acf":{"show_featured_image":true,"vf_locked":false,"featured":false,"article_intro":"<p>Multi-tasking protein provides new approaches for anti-tuberculosis drugs<\/p>\n","article_sources":[{"source_description":"<p>Due, A. V., Kuper, J., Geerlof, A., von Kries, J. P., &amp; Wilmanns, M. Bi-substrate specificity in histidine\/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis. <em>PNAS<\/em>, Early Online Publication 14 February 2011. DOI: 10.1073\/pnas.1015996108.<\/p>\n","source_link_url":"https:\/\/www.pnas.org\/content\/108\/9\/3554"}],"related_links":false,"in_this_article":false,"color":"#007B53","link_color":"#fff","youtube_url":"","mp4_url":"","video_caption":"","press_contact":"EMBL Generic","field_target_display":"embl","source_article":false},"embl_taxonomy_terms":[{"uuid":"a:3:{i:0;s:36:\"b14d3f13-5670-44fb-8970-e54dfd9c921a\";i:1;s:36:\"89e00fee-87f4-482e-a801-4c3548bb6a58\";i:2;s:36:\"613c4de5-1775-447f-af71-4b07085318e9\";}","parents":[],"name":["EMBL Hamburg"],"slug":"embl-hamburg","description":"Where &gt; All EMBL sites &gt; EMBL Hamburg"},{"uuid":"a:2:{i:0;s:36:\"4428d1fd-441a-4d6d-a1c5-5dcf5665f213\";i:1;s:36:\"c1800a73-a9f4-4389-887c-f069f4ebf475\";}","parents":[],"name":["Matthias Wilmanns"],"slug":"matthias-wilmanns","description":"Who &gt; Matthias Wilmanns"},{"uuid":"a:3:{i:0;s:36:\"302cfdf7-365b-462a-be65-82c7b783ebf7\";i:1;s:36:\"2dc39890-6c01-47bf-ac78-d42abdb10079\";i:2;s:36:\"b7081976-e7c1-4678-ab00-3e02d20e9e87\";}","parents":[],"name":["Wilmanns Group"],"slug":"wilmanns-group","description":"What &gt; Structural Biology (EMBL Hamburg) &gt; Wilmanns Group"}],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Two in one | EMBL<\/title>\n<meta name=\"description\" content=\"Multi-tasking enzyme from Mycobacterium tuberculosis provides new approaches for anti-tuberculosis drugs.\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science\/two-in-one\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Two in one | EMBL\" \/>\n<meta property=\"og:description\" content=\"Multi-tasking enzyme from Mycobacterium tuberculosis provides new approaches for anti-tuberculosis drugs.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/two-in-one\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:published_time\" content=\"2011-02-14T20:00:00+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-11-14T15:30:27+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2011\/02\/PriA.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"1000\" \/>\n\t<meta property=\"og:image:height\" content=\"600\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Guest author(s)\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@embl\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Guest author(s)\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"3 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/two-in-one\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/two-in-one\/\"},\"author\":{\"name\":\"Guest author(s)\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/b4d9366b2ebe691c4015c64c3619205b\"},\"headline\":\"Two in one\",\"datePublished\":\"2011-02-14T20:00:00+00:00\",\"dateModified\":\"2024-11-14T15:30:27+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/two-in-one\/\"},\"wordCount\":416,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/two-in-one\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2011\/02\/PriA.jpg\",\"keywords\":[\"enzyme\",\"hamburg\",\"press release\",\"tuberculosis\",\"wilmanns\"],\"articleSection\":[\"Science\",\"Science &amp; 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