Conformational Changes in a Macrolide Antibiotic Binding Protein From Mycobacterium smegmatis Upon ADP Binding

doi:10.3389/fmicb.2021.780954

	Conformational Changes in a Macrolide Antibiotic Binding Protein From Mycobacterium smegmatis Upon ADP Binding
	Zhang, Qingqing 1,2; Liu, Xiang 1; Liu, Huijuan 1; Zhang, Bingjie 3; Yang, Haitao4,5 ; Mi, Kaixia 3; Guddat, Luke W.6; Rao, Zihe1,4,5,7,8
	2021-12-09
发表期刊	FRONTIERS IN MICROBIOLOGY (IF:4.0[JCR-2023],5.1[5-Year])
EISSN	1664-302X
卷号	12
发表状态	已发表
DOI	10.3389/fmicb.2021.780954
摘要	Rv3197 (MABP-1), a non-canonical ABC protein in Mycobacterium tuberculosis, has ATPase activity and confers inducible resistance to the macrolide family of antibiotics. Here we have shown that MSMEG_1954, the homolog of Rv3197 in M. smegmatis, has a similar function of conferring macrolide resistance. Crystal structures of apo-MSMEG_1954 (form1 and form 2) and MSMEG_1954 in complex with ADP have been determined. These three structures show that MSMEG_1954 has at least two different conformations we identify as closed state (MSMEG_1954-form 1) and open state (MSMEG_1954-form 2 and MSMEG_1954-ADP). Structural superimposition shows that the MSMEG_1954-form 2 and MSMEG_1954-ADP complex have similar conformation to that observed for MABP-1 and MABP-1-erythromicin complex structure. However, the antibiotic binding pocket in MSMEG_1954-form 1 is completely blocked by the N-terminal accessory domain. When bound by ADP, the N-terminal accessory domain undergoes conformational change, which results in the open of the antibiotic binding pocket. Because of the degradation of N terminal accessory domain in MSMSG_1954-form 2, it is likely to represent a transitional state between MSMEG_1954-form 1 and MSMEG_1954-ADP complex structure.
关键词	crystal structure conformational change macrolide antibiotic binding protein (MABP) non-canonical ABC transporter macrolide antibiotic erythromycin
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收录类别	SCI ; SCIE
语种	英语
WOS研究方向	Microbiology
WOS类目	Microbiology
WOS记录号	WOS:000760982900001
出版者	FRONTIERS MEDIA SA
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/161441
专题	免疫化学研究所_PI研究组_杨海涛组生命科学与技术学院免疫化学研究所_特聘教授组_饶子和组
通讯作者	Liu, Xiang; Rao, Zihe
作者单位	1.Nankai Univ, Coll Life Sci, Frontiers Sci Ctr Cell Responses, State Key Lab Med Chem Biol, Tianjin, Peoples R China 2.Guangzhou Lab, Innovat Ctr Pathogen Res, Guangzhou, Peoples R China 3.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing, Peoples R China 4.ShanghaiTech Univ, Shanghai Inst Adv Immunochem Studies, Shanghai, Peoples R China 5.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China 6.Univ Queensland, Sch Chem & Mol Biosci, Brisbane, Qld, Australia 7.Tsinghua Univ, Sch Life Sci, Lab Struct Biol, Beijing, Peoples R China 8.Tsinghua Univ, Sch Med, Beijing, Peoples R China
通讯作者单位	免疫化学研究所; 生命科学与技术学院
推荐引用方式 GB/T 7714	Zhang, Qingqing,Liu, Xiang,Liu, Huijuan,et al. Conformational Changes in a Macrolide Antibiotic Binding Protein From Mycobacterium smegmatis Upon ADP Binding[J]. FRONTIERS IN MICROBIOLOGY,2021,12.
APA	Zhang, Qingqing.,Liu, Xiang.,Liu, Huijuan.,Zhang, Bingjie.,Yang, Haitao.,...&Rao, Zihe.(2021).Conformational Changes in a Macrolide Antibiotic Binding Protein From Mycobacterium smegmatis Upon ADP Binding.FRONTIERS IN MICROBIOLOGY,12.
MLA	Zhang, Qingqing,et al."Conformational Changes in a Macrolide Antibiotic Binding Protein From Mycobacterium smegmatis Upon ADP Binding".FRONTIERS IN MICROBIOLOGY 12(2021).