4Z7F

Crystal structure of FolT bound with folic acid

Summary for 4Z7F

• Entry DOI: 10.2210/pdb4z7f/pdb
• Descriptor: Folate ECF transporter, FOLIC ACID (2 entities in total)
• Functional Keywords: folate transporter, gating mechanism, folate binding and release, group ii ecf transporters, atp-binding cassette transporters, transport protein
• Biological source: Enterococcus faecalis (strain ATCC 700802 / V583)
• Total number of polymer chains: 6
• Total formula weight: 137394.88

Authors

Zhao, Q.,Wang, C.C.,Wang, C.Y.,Zhang, P. (deposition date: 2015-04-07, release date: 2015-07-29, Last modification date: 2024-10-23)

Primary citation

Zhao, Q.,Wang, C.C.,Wang, C.Y.,Guo, H.,Bao, Z.H.,Zhang, M.H.,Zhang, P.
Structures of FolT in substrate-bound and substrate-released conformations reveal a gating mechanism for ECF transporters
Nat Commun, 6:7661-7661, 2015

PubMed Abstract: 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-Å 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.

PubMed: 26198469
DOI: 10.1038/ncomms8661

Experimental method

X-RAY DIFFRACTION (3.194 Å)