{"title":"金黄色葡萄球菌的 DUF3055 采用独特策略实现结构独特性","authors":"Hyo Jung Kim, Hyoun Sook Kim","doi":"10.1186/s13765-024-00913-7","DOIUrl":null,"url":null,"abstract":"<div><p><i>Staphylococcus aureus</i> remains a public health threat with the WHO classifying the pathogen as a high priority in the development of new antimicrobial agents. Whole genome sequencing has revealed a number of conserved genes that may be essential for cell viability and infection. Characterising the structure and function of these proteins will inevitably aid development of new antimicrobials. Therefore, this study elucidated the structure of hypothetical protein DUF3055 from <i>S. aureus</i> stain Mu50. The protein possesses an as yet undefined function and a unique fold. The size of DUF3055 made it an ideal candidate for NMR characterisation which in conjunction with circular dichroism revealed the protein to be folded. Crystallisation and structural solution found that the overall dimer fold has a negatively charged surface formed by a β-bulge and tightly crossed α-helices, with a complementary size to a DNA single turn. Our structural observations suggest that hypothetical protein DUF3055 from <i>S. aureus</i> has a role in DNA binding and gene regulation.</p></div>","PeriodicalId":467,"journal":{"name":"Applied Biological Chemistry","volume":"67 1","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2024-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://applbiolchem.springeropen.com/counter/pdf/10.1186/s13765-024-00913-7","citationCount":"0","resultStr":"{\"title\":\"DUF3055 from Staphylococcus aureus adopts unique strategy for structural distinctiveness\",\"authors\":\"Hyo Jung Kim, Hyoun Sook Kim\",\"doi\":\"10.1186/s13765-024-00913-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><i>Staphylococcus aureus</i> remains a public health threat with the WHO classifying the pathogen as a high priority in the development of new antimicrobial agents. Whole genome sequencing has revealed a number of conserved genes that may be essential for cell viability and infection. Characterising the structure and function of these proteins will inevitably aid development of new antimicrobials. Therefore, this study elucidated the structure of hypothetical protein DUF3055 from <i>S. aureus</i> stain Mu50. The protein possesses an as yet undefined function and a unique fold. The size of DUF3055 made it an ideal candidate for NMR characterisation which in conjunction with circular dichroism revealed the protein to be folded. Crystallisation and structural solution found that the overall dimer fold has a negatively charged surface formed by a β-bulge and tightly crossed α-helices, with a complementary size to a DNA single turn. Our structural observations suggest that hypothetical protein DUF3055 from <i>S. aureus</i> has a role in DNA binding and gene regulation.</p></div>\",\"PeriodicalId\":467,\"journal\":{\"name\":\"Applied Biological Chemistry\",\"volume\":\"67 1\",\"pages\":\"\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2024-07-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://applbiolchem.springeropen.com/counter/pdf/10.1186/s13765-024-00913-7\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Applied Biological Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://link.springer.com/article/10.1186/s13765-024-00913-7\",\"RegionNum\":3,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Biological Chemistry","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1186/s13765-024-00913-7","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
DUF3055 from Staphylococcus aureus adopts unique strategy for structural distinctiveness
Staphylococcus aureus remains a public health threat with the WHO classifying the pathogen as a high priority in the development of new antimicrobial agents. Whole genome sequencing has revealed a number of conserved genes that may be essential for cell viability and infection. Characterising the structure and function of these proteins will inevitably aid development of new antimicrobials. Therefore, this study elucidated the structure of hypothetical protein DUF3055 from S. aureus stain Mu50. The protein possesses an as yet undefined function and a unique fold. The size of DUF3055 made it an ideal candidate for NMR characterisation which in conjunction with circular dichroism revealed the protein to be folded. Crystallisation and structural solution found that the overall dimer fold has a negatively charged surface formed by a β-bulge and tightly crossed α-helices, with a complementary size to a DNA single turn. Our structural observations suggest that hypothetical protein DUF3055 from S. aureus has a role in DNA binding and gene regulation.
期刊介绍:
Applied Biological Chemistry aims to promote the interchange and dissemination of scientific data among researchers in the field of agricultural and biological chemistry. The journal covers biochemistry and molecular biology, medical and biomaterial science, food science, and environmental science as applied to multidisciplinary agriculture.