8G52

Crystal structure of a bacterial TPAT family transporter

Summary for 8G52

• Entry DOI: 10.2210/pdb8g52/pdb
• Descriptor: TPR_REGION domain-containing protein, PALMITIC ACID (3 entities in total)
• Functional Keywords: tpat family, lipid, transport, lipid binding protein
• Biological source: Enhygromyxa salina
• Total number of polymer chains: 2
• Total formula weight: 72539.67

Authors

Dassama, L.M.K.,Zhai, L. (deposition date: 2023-02-11, release date: 2023-05-24, Last modification date: 2024-11-06)

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

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: 37170829
DOI: 10.1002/cbic.202300156

Experimental method

X-RAY DIFFRACTION (1.88 Å)