CAS OpenIR  > 中科院上海应用物理研究所2011-2019年
Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters
Yu, Y; Zhou, MZ; Kirsch, F; Xu, CQ; Zhang, L; Wang, Y; Jiang, Z; Wang, N; Li, J; Eitinger, T; Yang, MJ; junli@tsinghua.edu.cn; thomas.eitinger@cms.hu-berlin.de; maojunyang@tsinghua.edu.cn
2014
Source PublicationCELL RESEARCH
ISSN1001-0602
Volume24Issue:3Pages:267—277
AbstractThe energy-coupling factor (ECF) transporters are multi-subunit protein complexes that mediate uptake of transition-metal ions and vitamins in about 50% of the prokaryotes, including bacteria and archaea. Biological and structural studies have been focused on ECF transporters for vitamins, but the molecular mechanism by which ECF systems transport metal ions from the environment remains unknown. Here we report the first crystal structure of a NikM, TtNikM2, the substrate-binding component (S component) of an ECF-type nickel transporter from Thermoanaerobacter tengcongensis. In contrast to the structures of the vitamin-specific S proteins with six transmembrane segments (TSs), TtNikM2 possesses an additional TS at its N-terminal region, resulting in an extracellular N-terminus. The highly conserved N-terminal loop inserts into the center of TtNikM2 and occludes a region corresponding to the substrate-binding sites of the vitamin-specific S components. Nickel binds to NikM via its coordination to four nitrogen atoms, which are derived from Met1, His2 and His67 residues. These nitrogen atoms form an approximately square-planar geometry, similar to that of the metal ion-binding sites in the amino-terminal Cu2+-and Ni2+-binding (ATCUN) motif. Replacements of residues in NikM contributing to nickel coordination compromised the Ni-transport activity. Furthermore, systematic quantum chemical investigation indicated that this geometry enables NikM to also selectively recognize Co2+. Indeed, the structure of TtNikM2 containing a bound Co2+ ion has almost no conformational change compared to the structure that contains a nickel ion. Together, our data reveal an evolutionarily conserved mechanism underlying the metal selectivity of EcfS proteins, and provide insights into the ion-translocation process mediated by ECF transporters.
KeywordCoupling Factor Transporter Crystal-structure Atcun Motif Abc Transporters Mg2++ Transporter Metal-binding Neuromedin-c Nickel Vitamin-b-12 Proteins
Indexed BySCI
Language英语
WOS IDWOS:000332246500005
Citation statistics
Cited Times:32[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/14318
Collection中科院上海应用物理研究所2011-2019年
Corresponding Authorjunli@tsinghua.edu.cn; thomas.eitinger@cms.hu-berlin.de; maojunyang@tsinghua.edu.cn
Recommended Citation
GB/T 7714
Yu, Y,Zhou, MZ,Kirsch, F,et al. Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters[J]. CELL RESEARCH,2014,24(3):267—277.
APA Yu, Y.,Zhou, MZ.,Kirsch, F.,Xu, CQ.,Zhang, L.,...&maojunyang@tsinghua.edu.cn.(2014).Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters.CELL RESEARCH,24(3),267—277.
MLA Yu, Y,et al."Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters".CELL RESEARCH 24.3(2014):267—277.
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