Crystal structure of the single-stranded DNA-binding protein SsbB in complex with the anticancer drug 5-fluorouracil: Extension of the 5-fluorouracil interactome to include the oligonucleotide/oligosaccharide-binding fold protein

doi:10.1016/j.bbrc.2020.11.125

中山醫學大學機構典藏 CSMUIR > 中山醫學大學研究成果 > 期刊論文 > Item 310902500/23943

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题名:	Crystal structure of the single-stranded DNA-binding protein SsbB in complex with the anticancer drug 5-fluorouracil: Extension of the 5-fluorouracil interactome to include the oligonucleotide/oligosaccharide-binding fold protein
作者:	Lin, ES;Huang, CY
关键词:	5-Fluorouracil;SsbB;Interactome;SSB;SsbA;Anticancer
日期:	2021
上传时间:	2022-08-05T09:45:20Z (UTC)
出版者:	ACADEMIC PRESS INC ELSEVIER SCIENCE
ISSN:	0006-291X
摘要:	Single-stranded DNA-binding proteins (SSBs) are essential to cells because they participate in DNA metabolic processes, such as DNA replication, repair, and recombination. Some bacteria possess more than one paralogous SSB. Three similar SSBs, namely, SsbA, SsbB, and SsbC, are found in Staphylococcus aureus. Whether the FDA-approved clinical drug 5-fluorouracil (5-FU) that is used to target the enzyme thymidylate synthase for anticancer therapy can also bind to SSBs remains unknown. In this study, we found that 5-FU could form a stable complex with S. aureus SsbB (SaSsbB). We cocrystallized 5-FU with SaSsbB and solved complex structures to assess binding modes. Two complex forms of the structures were determined, namely, the individual asymmetric unit (two SaSsbB monomers) containing one (PDB entry 7D8J) or two 5-FU molecules (PDB entry 7DEP). The locations of 5-FU in these two SaSsbB complexes were similar regardless of the binding ratio. The structures revealed that residues T12, K13, T30, F48, and N50 of SaSsbB were involved in 5-FU binding. The mutations of T12, K13, and F48 caused the low 5-FU binding activity of SaSsbB, a result consistent with the structural analysis results. Taken together, the complexed structure and the binding mode analysis of SaSsbB extended the anticancer drug 5-FU interactome to include the oligonucleotide/oligosaccharide-binding fold protein. (C) 2020 Elsevier Inc. All rights reserved.
URI:	http://dx.doi.org/10.1016/j.bbrc.2020.11.125 https://www.webofscience.com/wos/woscc/full-record/WOS:000607297600007 https://ir.csmu.edu.tw:8080/handle/310902500/23943
關聯:	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS ,2021,v534 , P41-46
显示于类别:	[中山醫學大學研究成果] 期刊論文

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