2jln | pdb_00002jln

Structure of Mhp1, a nucleobase-cation-symport-1 family transporter

spinqualitylabelsall models 2jln, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jln is a 1 chain structure with sequence from Microbacterium liquefaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.85Å Ligands: HG, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HYUP_MICLQ Nucleobase-proton symporter that mediates the sodium-dependent binding and uptake of 5-aryl-substituted hydantoin compounds (PubMed:16621827, PubMed:24952894). 5-indolyl methyl hydantoin and 5-benzyl hydantoin are the preferred substrates, with selectivity for a hydrophobic substituent in position 5 of hydantoin and for the L isomer over the D isomer (PubMed:16621827, PubMed:24952894). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The 'Nucleobase-Cation-Symport-1', NCS1, transporters are essential components of salvage pathways for nucleobases and related metabolites. Here, we report the 2.85 A resolution structure of the NCS1 benzyl-hydantoin transporter, Mhp1, from Microbacterium liquefaciens. Mhp1 contains 12 transmembrane helices, 10 of which are arranged in two inverted repeats of 5 helices. The structures of the outward-facing open and substrate-bound occluded conformations were solved, showing how the outward-facing cavity closes upon binding of substrate. Comparisons with the leucine (LeuTAa) and the galactose (vSGLT) transporters reveal that the outward- and inward-facing cavities are symmetrically arranged on opposite sides of the membrane. The reciprocal opening and closing of these cavities is synchronised by the inverted repeat helices 3 and 8, providing the structural basis of the 'alternating access' model for membrane transport. Structure and Molecular Mechanism of a Nucleobase-Cation-Symport-1 Family Transporter.,Weyand S, Shimamura T, Yajima S, Suzuki S, Mirza O, Krusong K, Carpenter EP, Rutherford NG, Hadden JM, O'Reilly J, Ma P, Saidijam M, Patching SG, Hope RJ, Norbertczak HT, Roach PC, Iwata S, Henderson PJ, Cameron AD Science. 2008 Oct 16. PMID:18927357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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