5jsz | pdb_00005jsz

Folate ECF transporter: apo state

spinqualitylabelsall models 5jsz, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jsz is a 8 chain structure. This structure supersedes the now removed PDB entry 5d7t. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5d7t Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [A0A061BSU4_LACDE] Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.[HAMAP-Rule:MF_01461] [ECFA1_LACDA] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. [ECFA2_LACDA] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. Publication Abstract from PubMed Energy-coupling factor (ECF) transporters mediate uptake of micronutrients in prokaryotes. The transporters consist of an S-component that binds the transported substrate and an ECF module (EcfAA'T) that binds and hydrolyses ATP. The mechanism of transport is poorly understood but presumably involves an unusual step in which the membrane-embedded S-component topples over to carry the substrate across the membrane. In many ECF transporters, the S-component dissociates from the ECF module after transport. Subsequently, substrate-bound S-components out-compete the empty proteins for re-binding to the ECF module in a new round of transport. Here we present crystal structures of the folate-specific transporter ECF-FolT from Lactobacillus delbrueckii. Interaction of the ECF module with FolT stabilizes the toppled state, and simultaneously destroys the high-affinity folate-binding site, allowing substrate release into the cytosol. We hypothesize that differences in the kinetics of toppling can explain how substrate-loaded FolT out-competes apo-FolT for association with the ECF module. Structural insight in the toppling mechanism of an energy-coupling factor transporter.,Swier LJ, Guskov A, Slotboom DJ Nat Commun. 2016 Mar 30;7:11072. doi: 10.1038/ncomms11072. PMID:27026363 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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