Structures and Mechanisms of a Novel Bacterial Transport System for Fatty Acids
- Department of Chemistry and Sarafan ChEM−H Institute Stanford University Stanford CA 94305 USA, Current address: School of Life Sciences The Chinese University of Hong Kong, Shatin New Territories Hong Kong China
- Department of Chemistry and Sarafan ChEM−H Institute Stanford University Stanford CA 94305 USA
- Department of Chemistry and Sarafan ChEM−H Institute Stanford University Stanford CA 94305 USA, Department of Microbiology and Immunology Stanford School of Medicine Stanford CA 94305 USA
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.
- Sponsoring Organization:
- USDOE
- Grant/Contract Number:
- NONE; AC02-76SF00515
- OSTI ID:
- 1988324
- Alternate ID(s):
- OSTI ID: 1993344; OSTI ID: 1998183
- Journal Information:
- ChemBioChem: a European journal of chemical biology, Journal Name: ChemBioChem: a European journal of chemical biology Journal Issue: 15 Vol. 24; ISSN 1439-4227
- Publisher:
- Wiley Blackwell (John Wiley & Sons)Copyright Statement
- Country of Publication:
- France
- Language:
- English
Similar Records
Evidence for posttranslational protein flavinylation in the syphilis spirochete Treponema pallidum: Structural and biochemical insights from the catalytic core of a periplasmic flavin-trafficking protein
Structural, Bioinformatic, and In Vivo Analyses of Two Treponema pallidum Lipoproteins Reveal a Unique TRAP Transporter