8G53
Crystal structure of a bacterial TPAT family transporter
Summary for 8G53
| Entry DOI | 10.2210/pdb8g53/pdb |
| Descriptor | TPR_REGION domain-containing protein (2 entities in total) |
| Functional Keywords | transporter, lipid binding protein, sterols |
| Biological source | Enhygromyxa salina |
| Total number of polymer chains | 1 |
| Total formula weight | 22598.34 |
| Authors | Dassama, L.M.K.,Zhai, L. (deposition date: 2023-02-11, release date: 2023-05-24, Last modification date: 2024-10-16) |
| Primary citation | Zhai, L.,Chou, J.C.,Oo, H.,Dassama, L.M.K. Structures and Mechanisms of a Novel Bacterial Transport System for Fatty Acids. Chembiochem, 24:e202300156-e202300156, 2023 Cited by PubMed Abstract: Bacterial acquisition of metabolites is largely facilitated by transporters with unique substrate scopes. The tripartite ATP-independent periplasmic (TRAP) transporters comprise a large family of bacterial proteins that facilitate the uptake of a variety of small molecules. It has been reported that some TRAP systems encode a fourth protein, the T component. The T-component, or TatT, is predicted to be a periplasmic-facing lipoprotein that enables the uptake of metabolites from the outer membrane. However, no substrates were revealed for any TatT and their functional role(s) remained enigmatic. We recently identified a homolog in Methylococcus capsulatus that binds to sterols, and herein, we report two additional homologs that demonstrate a preference for long-chain fatty acids. Our bioinformatics, quantitative analyses of protein-ligand interactions, and high-resolution crystal structures suggest that TatTs might facilitate the trafficking of hydrophobic or lipophilic substrates and represent a new class of bacterial lipid and fatty acid transporters. PubMed: 37170829DOI: 10.1002/cbic.202300156 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.03 Å) |
Structure validation
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