The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Structure of a cation-bound multidrug and toxic compound extrusion transporter
Open accessAbstract
Transporter proteins from the MATE (multidrug and toxic compound extrusion) family are vital in metabolite transport in plants, directly affecting crop yields worldwide. MATE transporters also mediate multiple-drug resistance (MDR) in bacteria and mammals, modulating the efficacy of many pharmaceutical drugs used in the treatment of a variety of diseases. MATE transporters couple substrate transport to electrochemical gradients and are the only remaining class of MDR transporters whose structure has not been determined. Here we report the X-ray structure of the MATE transporter NorM from Vibrio cholerae determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known MDR transporter. We also report a cation-binding site in close proximity to residues previously deemed critical for transport. This conformation probably represents a stage of the transport cycle with high affinity for monovalent cations and low affinity for substrates.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
Automated MAD and MIR structure solution
Terwilliger, T. C., & Berendzen, J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999000839 · Cited by 3,036
Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding
Aller, S. G., Yu, J., Ward, A., Weng, Y., Chittaboina, S., Zhuo, R., Harrell, P. M., Trinh, Y. T., Zhang, Q., Urbatsch, I. L., et al. (2009) · Science · doi:10.1126/science.1168750 · Cited by 1,929
Self-citationMaximum-likelihood density modification
Terwilliger, T. C. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900005072 · Cited by 1,634
Structure and Mechanism of the Lactose Permease of Escherichia coli
Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R., & Iwata, S. (2003) · Science · doi:10.1126/science.1088196 · Cited by 1,389
Version 1.2 of the Crystallography and NMR system
Brunger, A. T. (2007) · Nature Protocols · doi:10.1038/nprot.2007.406 · Cited by 1,336
Cited by
Ribosome-targeting antibiotics and mechanisms of bacterial resistance
Wilson, D. N. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3155 · Cited by 1,054
Multidrug efflux pumps in Gram-negative bacteria and their role in antibiotic resistance.
Blair, J. M., Richmond, G. E., & Piddock, L. J. (2014) · Future Microbiology · doi:10.2217/fmb.14.66 · Cited by 481
Flavonoid transport mechanisms: how to go, and with whom
Zhao, J. (2015) · Trends in Plant Science · doi:10.1016/j.tplants.2015.06.007 · Cited by 393
Cu Homeostasis in Bacteria: The Ins and Outs
Andrei, A., Öztürk, Y., Khalfaoui-Hassani, B., Rauch, J., Marckmann, D., Trasnea, P.-I., Daldal, F., & Koch, H.-G. (2020) · Membranes · doi:10.3390/membranes10090242 · Cited by 153
Structural Symmetry in Membrane Proteins
Forrest, L. R. (2015) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-051013-023008 · Cited by 148
Metadata
- Authors
- He, X., Szewczyk, P., Karyakin, A., Evin, M., Hong, W.-X., Zhang, Q., & Chang, G.
- Venue
- Nature
- Published
- 2010-09-22
- Volume
- 467
- Issue
- 7318
- Pages
- 991-994
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1992956599
- Cited by
- 272
- References
- 35
- FWCI
- 7.98
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Structure of a cation-bound multidrug and toxic compound extrusion transporter. https://app.cochat.ai/papers/10.1038/nature09408
- The paper
- He, X., Szewczyk, P., Karyakin, A., Evin, M., Hong, W.-X., Zhang, Q., & Chang, G. (2010). Structure of a cation-bound multidrug and toxic compound extrusion transporter. Nature. https://doi.org/10.1038/nature09408
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
