Proteopedia

2jln

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

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:,
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).[1] [2] [3]

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[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Suzuki S, Henderson PJ. The hydantoin transport protein from Microbacterium liquefaciens. J Bacteriol. 2006 May;188(9):3329-36. doi: 10.1128/JB.188.9.3329-3336.2006. PMID:16621827 doi:http://dx.doi.org/10.1128/JB.188.9.3329-3336.2006
  2. ↑ Simmons KJ, Jackson SM, Brueckner F, Patching SG, Beckstein O, Ivanova E, Geng T, Weyand S, Drew D, Lanigan J, Sharples DJ, Sansom MS, Iwata S, Fishwick CW, Johnson AP, Cameron AD, Henderson PJ. Molecular mechanism of ligand recognition by membrane transport protein, Mhp1. EMBO J. 2014 Jun 21. pii: e201387557. PMID:24952894 doi:http://dx.doi.org/10.15252/embj.201387557
  3. ↑ Suzuki S, Takenaka Y, Onishi N, Yokozeki K. Molecular cloning and expression of the hyu genes from Microbacterium liquefaciens AJ 3912, responsible for the conversion of 5-substituted hydantoins to alpha-amino acids, in Escherichia coli. Biosci Biotechnol Biochem. 2005 Aug;69(8):1473-82. doi: 10.1271/bbb.69.1473. PMID:16116274 doi:http://dx.doi.org/10.1271/bbb.69.1473
  4. ↑ 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. Structure and Molecular Mechanism of a Nucleobase-Cation-Symport-1 Family Transporter. Science. 2008 Oct 16. PMID:18927357

2jln, resolution 2.85Å

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OCA
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