Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter. / Weyand, Simone; Shimamura, Tatsuro; Yajima, Shunsuke; Suzuki, Shun'ichi; Mirza, Osman Asghar; Krusong, Kuakarun; Carpenter, Elisabeth P; Rutherford, Nicholas G; Hadden, Jonathan M; O'Reilly, John; Ma, Pikyee; Saidijam, Massoud; Patching, Simon G; Hope, Ryan J; Norbertczak, Halina T; Roach, Peter C J; Iwata, So; Henderson, Peter J F; Cameron, Alexander D.
I: Science, Bind 322, Nr. 5902, 2008, s. 709-713.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter
AU - Weyand, Simone
AU - Shimamura, Tatsuro
AU - Yajima, Shunsuke
AU - Suzuki, Shun'ichi
AU - Mirza, Osman Asghar
AU - Krusong, Kuakarun
AU - Carpenter, Elisabeth P
AU - Rutherford, Nicholas G
AU - Hadden, Jonathan M
AU - O'Reilly, John
AU - Ma, Pikyee
AU - Saidijam, Massoud
AU - Patching, Simon G
AU - Hope, Ryan J
AU - Norbertczak, Halina T
AU - Roach, Peter C J
AU - Iwata, So
AU - Henderson, Peter J F
AU - Cameron, Alexander D
N1 - Keywords: Actinomycetales; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Cations; Cell Membrane; Crystallography, X-Ray; Hydantoins; Ion Transport; Models, Molecular; Molecular Sequence Data; Nucleobase Transport Proteins; Protein Conformation; Protein Structure, Secondary; Sodium; Symporters
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
KW - Former Faculty of Pharmaceutical Sciences
U2 - 10.1126/science.1164440
DO - 10.1126/science.1164440
M3 - Journal article
C2 - 18927357
VL - 322
SP - 709
EP - 713
JO - Science
JF - Science
SN - 0036-8075
IS - 5902
ER -
ID: 10488112