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Fig. 1 | BMC Biology

Fig. 1

From: High-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding

Fig. 1

Overall structure of AdiC from E. coli in the outward-open conformation. The structure is represented as ribbon and transparent surface, and viewed from the membrane plane (A), rotated by 75° (B) and from the periplasmic side (C). Individual monomers are shown with different shades of blue and yellow. Both termini are located on the cytoplasmic side and are indicated with the corresponding colored capital letters N and C. The twelve TMs of each monomer are represented by cylinders and labeled TM1-TM12. TM1 and TM6 are discontinuous, and each consists of two short α-helices (labeled TM1a and TM1b, and TM6a and TM6b). TMs 1-10 (light blue and yellow) adopt the 5+5 inverted repeats topology and form a barrel-like structure, which is best seen in the surface representation of the right monomer in B. TMs 11 and 12 (blue and light orange) constitute most of the homodimer interface

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BMC Biology

ISSN: 1741-7007

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