Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate

doi:10.1038/s41422-018-0032-8

	Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate
	Qiu, Biao1,2 ; Xia, Bingqing 3,9; Zhou, Qingtong4 ; Lu, Yan1,2 ; He, Miaomiao1,2 ; Hasegawa, Kazuya 5; Ma, Zhiqiang 6; Zhang, Fengyu 7; Gu, Lichuan 7; Mao, Qionglei 3,9; Wang, Feng 8; Zhao, Suwen1,4 ; Gao, Zhaobing 3; Liao, Jun1,2
	2018-06
发表期刊	CELL RESEARCH (IF:28.1[JCR-2023],36.4[5-Year])
ISSN	1001-0602
卷号	28 期号:6 页码:644-654
发表状态	已发表
DOI	10.1038/s41422-018-0032-8
摘要	Acetate is an important metabolite in metabolism and cell signaling. Succinate-Acetate Permease (SatP) superfamily proteins are known to be responsible for acetate transport across membranes, but the nature of this transport remains unknown. Here, we show that the SatP homolog from Citrobacter koseri (SatP_Ck) is an anion channel that can unidirectionally translocate acetate at rates of the order of similar to 10(7) ions/s. Crystal structures of SatP_Ck in complex with multiple acetates at 1.8 angstrom reveal that the acetate pathway consists of four acetate-binding sites aligned in a single file that are interrupted by three hydrophobic constrictions. The bound acetates at the four sites are each orientated differently. The acetate at the cytoplasmic vestibule is partially dehydrated, whereas those in the main pore body are fully dehydrated. Aromatic residues within the substrate pathway may coordinate translocation of acetates via anion-p interactions. SatP_Ck reveals a new type of selective anion channel and provides a structural and functional template for understanding organic anion transport.
收录类别	SCI ; SCIE ; CSCD
语种	英语
资助项目	China Post-Doctoral Science Foundation[2016M600344]
WOS研究方向	Cell Biology
WOS类目	Cell Biology
WOS记录号	WOS:000434816300007
CSCD记录号	CSCD:6266442
出版者	NATURE PUBLISHING GROUP
WOS关键词	CHAIN FATTY-ACIDS ; CHLORIDE CHANNEL ; MOLECULAR-BASIS ; ACETIC-ACID ; PROTEIN ; TRANSPORTER ; ACETYLATION ; REVEALS ; TOOL ; INTEGRATION
原始文献类型	Article
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/23079
专题	生命科学与技术学院生命科学与技术学院_PI研究组_廖军组 iHuman研究所_特聘教授组_Andrej Sali组 iHuman研究所_PI研究组_赵素文组生命科学与技术学院_硕士生
通讯作者	Gao, Zhaobing; Liao, Jun
作者单位	1.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China 2.Chinese Acad Sci, Inst Biochem & Cell Biol, 320 Yueyang Rd, Shanghai 200031, Peoples R China 3.Chinese Acad Sci, CAS Key Lab Receptor Res, State Key Lab Drug Res, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China 4.ShanghaiTech Univ, iHuman Inst, Shanghai 201210, Peoples R China 5.Japan Synchrotron Radiat Res Inst, Prot Crystal Anal Div, Sayo, Hyogo 6795198, Japan 6.South China Univ Technol, Key Lab Funct Mol Engn Guangdong Prov, Sch Chem & Chem Engn, Guangzhou 510640, Guangdong, Peoples R China 7.Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Shandong, Peoples R China 8.Wuxi Biortus Biosci Co Ltd, Wuxi 214437, Jiangsu, Peoples R China 9.Univ Chinese Acad Sci, 19A Yuquan Rd, Beijing 100049, Peoples R China
第一作者单位	生命科学与技术学院
通讯作者单位	生命科学与技术学院
第一作者的第一单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Qiu, Biao,Xia, Bingqing,Zhou, Qingtong,et al. Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate[J]. CELL RESEARCH,2018,28(6):644-654.
APA	Qiu, Biao.,Xia, Bingqing.,Zhou, Qingtong.,Lu, Yan.,He, Miaomiao.,...&Liao, Jun.(2018).Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate.CELL RESEARCH,28(6),644-654.
MLA	Qiu, Biao,et al."Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate".CELL RESEARCH 28.6(2018):644-654.