2JLN

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

Summary for 2JLN

• Entry DOI: 10.2210/pdb2jln/pdb
• Related: 2JLO
• Descriptor: MHP1, SODIUM ION, MERCURY (II) ION (3 entities in total)
• Functional Keywords: hydantoin, transporter, membrane protein, nucleobase-cation-symport-1 family
• Biological source: MICROBACTERIUM LIQUEFACIENS
• Total number of polymer chains: 1
• Total formula weight: 54842.37

Authors

Weyand, S.,Shimamura, T.,Yajima, S.,Suzuki, S.,Mirza, O.,Krusong, K.,Carpenter, E.P.,Rutherford, N.G.,Hadden, J.M.,O'Reilly, J.,Ma, P.,Saidijam, M.,Patching, S.G.,Hope, R.J.,Norbertczak, H.T.,Roach, P.C.J.,Iwata, S.,Henderson, P.J.F.,Cameron, A.D. (deposition date: 2008-09-11, release date: 2008-10-28, Last modification date: 2024-05-08)

Primary citation

Weyand, S.,Shimamura, T.,Yajima, S.,Suzuki, S.,Mirza, O.,Krusong, K.,Carpenter, E.P.,Rutherford, N.G.,Hadden, J.M.,O'Reilly, J.,Ma, P.,Saidijam, M.,Patching, S.G.,Hope, R.J.,Norbertczak, H.T.,Roach, P.C.J.,Iwata, S.,Henderson, P.J.F.,Cameron, A.D.
Structure and Molecular Mechanism of a Nucleobase-Cation-Symport-1 Family Transporter.
Science, 322:709-, 2008

PubMed Abstract: The nucleobase-cation-symport-1 (NCS1) transporters are essential components of salvage pathways for nucleobases and related metabolites. Here, we report the 2.85-angstrom 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 five 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 transporter LeuT(Aa) and the galactose transporter vSGLT 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 synchronized by the inverted repeat helices 3 and 8, providing the structural basis of the alternating access model for membrane transport.

PubMed: 18927357
DOI: 10.1126/SCIENCE.1164440

Experimental method

X-RAY DIFFRACTION (2.85 Å)