The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural basis of a GatC ortholog transporter in the bacterial phosphotransferase system
Open accessPublished version of a preprint
Abstract
The bacterial phosphotransferase system (PTS) mediates the uptake of specific carbohydrates via IIC transporters. Here, we report the crystal and cryo‐electron microscopy (cryo‐EM) structures of Leminorella grimontii galactitol‐specific PTS enzyme IIC component (LgGatC), which is implicated in D‐xylose uptake and belongs to the ascorbate–galactitol (AG) superfamily of IIC proteins. These structures, determined in the presence and absence of D‐xylose, capture the transporter in an outward‐facing conformation. A homology model of an inward‐facing state, constructed based on these structures, supports an elevator‐like transport mechanism. These findings provide structural insights into substrate recognition by GatC and offer a framework for understanding sugar transport in PTS IIC proteins.
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
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Accurate structure prediction of biomolecular interactions with AlphaFold 3
Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861
Flagged first, then by citations
Research works printed but not linked: 38
- 10.1016/j.biotechadv.2012.03.002 · DOI
- 10.1186/s13068-020-1662-x · DOI
- 10.1016/j.ymben.2012.07.007 · DOI
- 10.1016/j.mcat.2024.114230 · DOI
- 10.1128/AEM.55.8.1943-1948.1989 · DOI
- 10.1007/s00253-006-0827-2 · DOI
- 10.1016/j.ymben.2011.05.005 · DOI
- 10.1073/pnas.1311970111 · DOI
- 10.1007/s00253-013-5401-0 · DOI
- 10.1007/BF02193633 · DOI
- 10.1016/S0923-2508(02)01339-6 · DOI
- 10.1128/MMBR.69.4.608-634.2005 · DOI
- 10.1007/s00424-020-02379-0 · DOI
- 10.1016/j.str.2016.04.003 · DOI
- 10.1073/pnas.1800647115 · DOI
- 10.1038/nature09939 · DOI
- 10.1038/nsmb.2975 · DOI
- 10.1038/s41421-018-0037-y · DOI
- 10.1038/s41422-019-0194-z · DOI
- 10.1038/s41467-024-52100-3 · DOI
- 10.1016/j.str.2006.01.013 · DOI
- 10.1093/protein/14.12.993 · DOI
- 10.1021/ja036166s · DOI
- 10.1038/nprot.2009.31 · DOI
- 10.1107/S2059798318017795 · DOI
- 10.1107/S2059798318004576 · DOI
- 10.1107/S0907444909047337 · DOI · Paper page
- 10.1107/S0021889807021206 · DOI · Paper page
- 10.1002/prot.26257 · DOI
- 10.1107/S0907444910007493 · DOI · Paper page
- 10.1107/S0907444909052925 · DOI · Paper page
- 10.1016/S0076-6879(09)64011-8 · DOI
- 10.1016/j.jsb.2005.07.007 · DOI
- 10.1038/nmeth.4169 · DOI · Paper page
- 10.1002/pro.3943 · DOI
- 10.1016/j.jsb.2016.10.002 · DOI
- 10.1093/nar/gky427 · DOI
- 10.1093/nar/gkr703 · DOI
Metadata
- Authors
- Takahashi, Y. S., Kohga, H., Chek, M. F., Yamamoto, K., Takahashi, J. F., Shigematsu, H., Tanaka, Y., Ichikawa, M., Miyazaki, R., Hakoshima, T., & Tsukazaki, T.
- Affiliations
- Nara Institute of Science and Technology (JP)
- Japan Synchrotron Radiation Research Institute (JP)
- Fudan University (CN)
- Corresponding author
- Tsukazaki, Tomoya
- ORCID
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2025-08
- Volume
- 599
- Issue
- 16
- Pages
- 2377-2387
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W4413002686
- Cited by
- 1
- References
- 2
- Citations by year
- 2026: 1
- FWCI
- 0.21
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- FEBS Letters (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (acceptedVersion)
- Funders
- Natural Science Foundation of Shanghai Municipality (24ZR1403800)
- Takeda Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- galactitol, transporter conformation, substrate recognition, sugar transport, homology model
- MeSH terms
- Bacterial Proteins, Models, Molecular, Phosphoenolpyruvate Sugar Phosphotransferase System, Protein Conformation, Xylose, Crystallography, X-Ray, Cryoelectron Microscopy, Planctomycetales
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