Language
English
Publication Date
8-15-2023
Journal
Proceedings of the National Academy of Sciences of the United States of America
DOI
10.1073/pnas.2302799120
PMID
37549264
PMCID
PMC10438392
PubMedCentral® Posted Date
8-7-2023
PubMedCentral® Full Text Version
Post-print
Abstract
The nucleobase/ascorbic acid transporter (NAT) family comprises proteins in all kingdoms of life. Their substrates, nucleobases and their analogs, have special attention in therapeutic applications, such as the treatment of solid tumors, lymphoproliferative diseases, viral infections, and inflammatory diseases. Here, we present the crystal structure of a bacterial NAT member, PurT of Colwellia psychrerythraea (PurTCp) at 2.80 Å resolution that, together with functional data, provide insight into the transport mechanism of NAT family members.
Keywords
Animals, Biological Transport, Purines, Mutation, Binding Sites, Ascorbic Acid, Mammals, PurTCp, NAT gene family, H+-coupled transport, nucleobases, X-ray crystallography
Published Open-Access
yes
Recommended Citation
Weng, Jun; Zhou, Xiaoming; Wiriyasermkul, Pattama; et al., "Insight Into the Mechanism of H+-Coupled Nucleobase Transport" (2023). Faculty and Staff Publications. 3872.
https://digitalcommons.library.tmc.edu/baylor_docs/3872