8g52 | pdb_00008g52

Crystal structure of a bacterial TPAT family transporter

spinqualitylabelsall models 8g52, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8g52 is a 2 chain structure with sequence from Enhygromyxa salina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Ligands: PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0C2DGE5_9DELT Publication Abstract from PubMed 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. Structures and mechanisms of a novel bacterial transport system for fatty acids.,Zhai L, Chou JC, Oo H, Dassama L Chembiochem. 2023 May 12:e202300156. doi: 10.1002/cbic.202300156. PMID:37170829 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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