ArticleCell research2014
Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters.
Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 43 citations in OpenAlex.
- Identification of inhibitors targeting the energy-coupling factor (ECF) transporters.Communications biology · 2023Article
- ATP-Binding Cassette Transporters: Snap-on Complexes?Sub-cellular biochemistry · 2022Article
- Metal utilization in genome-reduced bacteria: Do human mycoplasmas rely on iron?Computational and structural biotechnology journal · 2021Review
- Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020Review
- Article
- The effect of an engineered ATCUN motif on the structure and biophysical properties of the SH3 domain of c-Src tyrosine kinase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Inhibition of urease activity by different compounds provides insight into the modulation and association of bacterial nickel import and ureolysis.Scientific reports · 2020Article
- Bimodal Nickel-Binding Site onInorganic chemistry · 2019Article
- Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR.International journal of molecular sciences · 2018Article
- Nickel Sequestration by the Host-Defense Protein Human Calprotectin.Journal of the American Chemical Society · 2017Article
- Structure and mechanism of a group-I cobalt energy coupling factor transporter.Cell research · 2017Article
- An Aromatic Cap Seals the Substrate Binding Site in an ECF-Type S Subunit for Riboflavin.Journal of molecular biology · 2016Article
- Crystal Structure of a Group I Energy Coupling Factor Vitamin Transporter S Component in Complex with Its Cognate Substrate.Cell chemical biology · 2016Article
- Structural insight in the toppling mechanism of an energy-coupling factor transporter.Nature communications · 2016Article
- Structures of FolT in substrate-bound and substrate-released conformations reveal a gating mechanism for ECF transporters.Nature communications · 2015Article
- ATP-dependent Conformational Changes Trigger Substrate Capture and Release by an ECF-type Biotin Transporter.The Journal of biological chemistry · 2015Article
- Pyridoxamine is a substrate of the energy-coupling factor transporter HmpT.Cell discovery · 2015Article
- Structural diversity of ABC transporters.The Journal of general physiology · 2014Review
- Diversity in ABC transporters: type I, II and III importers.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 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 Cu(2+)- and Ni(2+)-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 Co(2+). Indeed, the structure of TtNikM2 containing a bound Co(2+) 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.
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