Gwan Hee Lee , Subin Kim , Do Yeon Kim , Ju Hee Han , So Yeon Lee , Jun Hyuck Lee , Chang Sup Lee , Hyun Ho Park
{"title":"脓肿分枝杆菌 MltG 的结构揭示了组成结构域之间的结构可塑性。","authors":"Gwan Hee Lee , Subin Kim , Do Yeon Kim , Ju Hee Han , So Yeon Lee , Jun Hyuck Lee , Chang Sup Lee , Hyun Ho Park","doi":"10.1107/S2052252524008443","DOIUrl":null,"url":null,"abstract":"<div><div>We provide the structure of MltG of the lytic transglycosylase family in this study. We show that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of <em>Mycobacterium abscessus</em> MltG has been revealed using structural analysis and sequence comparison. This research significantly advances our comprehension of the transglycosylation process mediated by the MltG family, providing valuable insights that can inform the development of next-generation antibiotics to specifically target <em>M. abscessus</em>.</div></div><div><div>MltG, a membrane-bound lytic transglycosylase, has roles in terminating glycan polymerization in peptidoglycan and incorporating glycan chains into the cell wall, making it significant in bacterial cell-wall biosynthesis and remodeling. This study provides the first reported MltG structure from <em>Mycobacterium abscessus</em> (maMltG), a superbug that has high antibiotic resistance. Our structural and biochemical analyses revealed that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of maMltG was disclosed using structural analysis and sequence comparison. Overall, this study contributes to our understanding of the transglycosylation reaction of the MltG family, aiding the design of next-generation antibiotics targeting <em>M. abscessus.</em></div></div>","PeriodicalId":14775,"journal":{"name":"IUCrJ","volume":"11 6","pages":"Pages 903-909"},"PeriodicalIF":2.9000,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11533991/pdf/","citationCount":"0","resultStr":"{\"title\":\"Structure of MltG from Mycobacterium abscessus reveals structural plasticity between composed domains\",\"authors\":\"Gwan Hee Lee , Subin Kim , Do Yeon Kim , Ju Hee Han , So Yeon Lee , Jun Hyuck Lee , Chang Sup Lee , Hyun Ho Park\",\"doi\":\"10.1107/S2052252524008443\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>We provide the structure of MltG of the lytic transglycosylase family in this study. We show that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of <em>Mycobacterium abscessus</em> MltG has been revealed using structural analysis and sequence comparison. This research significantly advances our comprehension of the transglycosylation process mediated by the MltG family, providing valuable insights that can inform the development of next-generation antibiotics to specifically target <em>M. abscessus</em>.</div></div><div><div>MltG, a membrane-bound lytic transglycosylase, has roles in terminating glycan polymerization in peptidoglycan and incorporating glycan chains into the cell wall, making it significant in bacterial cell-wall biosynthesis and remodeling. This study provides the first reported MltG structure from <em>Mycobacterium abscessus</em> (maMltG), a superbug that has high antibiotic resistance. Our structural and biochemical analyses revealed that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of maMltG was disclosed using structural analysis and sequence comparison. Overall, this study contributes to our understanding of the transglycosylation reaction of the MltG family, aiding the design of next-generation antibiotics targeting <em>M. abscessus.</em></div></div>\",\"PeriodicalId\":14775,\"journal\":{\"name\":\"IUCrJ\",\"volume\":\"11 6\",\"pages\":\"Pages 903-909\"},\"PeriodicalIF\":2.9000,\"publicationDate\":\"2024-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11533991/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"IUCrJ\",\"FirstCategoryId\":\"88\",\"ListUrlMain\":\"https://www.sciencedirect.com/org/science/article/pii/S2052252524000915\",\"RegionNum\":2,\"RegionCategory\":\"材料科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"IUCrJ","FirstCategoryId":"88","ListUrlMain":"https://www.sciencedirect.com/org/science/article/pii/S2052252524000915","RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Structure of MltG from Mycobacterium abscessus reveals structural plasticity between composed domains
We provide the structure of MltG of the lytic transglycosylase family in this study. We show that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of Mycobacterium abscessus MltG has been revealed using structural analysis and sequence comparison. This research significantly advances our comprehension of the transglycosylation process mediated by the MltG family, providing valuable insights that can inform the development of next-generation antibiotics to specifically target M. abscessus.
MltG, a membrane-bound lytic transglycosylase, has roles in terminating glycan polymerization in peptidoglycan and incorporating glycan chains into the cell wall, making it significant in bacterial cell-wall biosynthesis and remodeling. This study provides the first reported MltG structure from Mycobacterium abscessus (maMltG), a superbug that has high antibiotic resistance. Our structural and biochemical analyses revealed that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of maMltG was disclosed using structural analysis and sequence comparison. Overall, this study contributes to our understanding of the transglycosylation reaction of the MltG family, aiding the design of next-generation antibiotics targeting M. abscessus.
期刊介绍:
IUCrJ is a new fully open-access peer-reviewed journal from the International Union of Crystallography (IUCr).
The journal will publish high-profile articles on all aspects of the sciences and technologies supported by the IUCr via its commissions, including emerging fields where structural results underpin the science reported in the article. Our aim is to make IUCrJ the natural home for high-quality structural science results. Chemists, biologists, physicists and material scientists will be actively encouraged to report their structural studies in IUCrJ.