Structural highlights
Publication Abstract from PubMed
Energy-coupling factor (ECF) transporters are a new family of ABC transporters that consist of four subunits, two cytoplasmic ATPases EcfA and EcfA' and two transmembrane proteins namely EcfS for substrate-specific binding and EcfT for energy coupling. Here, we report the 3.2-A resolution crystal structure of the EcfS protein of a folate ECF transporter from Enterococcus faecalis-EfFolT, a close homologue of FolT from Lactobacillus brevis-LbFolT. Structural and biochemical analyses reveal the residues constituting the folate-binding pocket and determining the substrate-binding specificity. Structural comparison of the folate-bound EfFolT with the folate-free LbFolT contained in the holotransporter complex discloses significant conformational change at the L1 loop, and reveals a gating mechanism of ECF transporters in which the L1 loop of EcfS acts as a gate in the substrate binding and release.
Structures of FolT in substrate-bound and substrate-released conformations reveal a gating mechanism for ECF transporters.,Zhao Q, Wang C, Wang C, Guo H, Bao Z, Zhang M, Zhang P Nat Commun. 2015 Jul 22;6:7661. doi: 10.1038/ncomms8661. PMID:26198469[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao Q, Wang C, Wang C, Guo H, Bao Z, Zhang M, Zhang P. Structures of FolT in substrate-bound and substrate-released conformations reveal a gating mechanism for ECF transporters. Nat Commun. 2015 Jul 22;6:7661. doi: 10.1038/ncomms8661. PMID:26198469 doi:http://dx.doi.org/10.1038/ncomms8661
