6jkd | pdb_00006jkd

Crystal structure of tetrameric PepTSo2 in I4 space group

spinqualitylabelsall models 6jkd, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jkd is a 1 chain structure with sequence from Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8EHE6_SHEON Publication Abstract from PubMed Proton-dependent oligopeptide transporters (POTs) belong to the major facilitator superfamily (MFS) and transport dipeptides and tripeptides from the extracellular environment into the target cell. The human POTs PepT1 and PepT2 are also involved in the absorption of various orally ingested drugs. Previously reported structures revealed that the bacterial POTs possess 14 helices, of which H1-H6 and H7-H12 constitute the typical MFS fold and the residual two helices are involved in the cytoplasmic linker. PepTSo2 from Shewanella oneidensis is a unique POT which reportedly assembles as a 200 kDa tetramer. Although the previously reported structures suggested the importance of H12 for tetramer formation, the structural basis for the PepTSo2-specific oligomerization remains unclear owing to the lack of a high-resolution tetrameric structure. In this study, the expression and purification conditions for tetrameric PepTSo2 were optimized. A single-particle cryo-EM analysis revealed the tetrameric structure of PepTSo2 incorporated into Salipro nanoparticles at 4.1 A resolution. Furthermore, a combination of lipidic cubic phase (LCP) crystallization and an automated data-processing system for multiple microcrystals enabled crystal structures of PepTSo2 to be determined at resolutions of 3.5 and 3.9 A. The present structures in a lipid bilayer revealed the detailed mechanism for the tetrameric assembly of PepTSo2, in which a characteristic extracellular loop (ECL) interacts with two asparagine residues on H12 which were reported to be important for tetramerization and plays an essential role in oligomeric assembly. This study provides valuable insights into the oligomerization mechanism of this MFS-type transporter, which will further pave the way for understanding other oligomeric membrane proteins. Structural basis for oligomerization of the prokaryotic peptide transporter PepTSo2.,Nagamura R, Fukuda M, Kawamoto A, Matoba K, Dohmae N, Ishitani R, Takagi J, Nureki O Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):348-358. doi:, 10.1107/S2053230X19003546. Epub 2019 Apr 24. PMID:31045564 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Symporter 3D structures

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