Fig. 5 | Nature Communications

Fig. 5

From: Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site

Fig. 5

Sodium and substrate binding sites of Na+ transporters that adopt the LeuT fold. a SiaT (outward-open, pdbid: 5NV9), b vSGLT (inward-open, pdbid: 3DH4), c Mhp1 (outward-occluded, pdbid: 4D1B), d BetP (Asp153Gly outward-open, pdbid: 4LLH), e LeuT (outward-occluded, pdbid: 2A65), f dDAT (N-terminally truncated, EL2 deleted, Val74Aala, Val275Ala, Val311Ala, Leu415Ala, Gly538Leu, pdbid: 4M48) and f SERT (outward-open, Tyr110Ala, Ile291Ala, Thr439Ser, Cys554Ala, Cys580Ala, Cys622Ala, pdbid: 5I71). Substrates and amino-acid residues coordinating the Na+ ions are represented in sticks with carbon atoms in grey or white, respectively. Residues surrounding the putative Na1´ in BetP are shown in sticks (d). Oxygen atoms are red and nitrogen atoms are blue. The Na+ ions are represented as blue spheres

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