Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for α-keto acid binding |
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Authors: | Sophie Gonin Pascal Arnoux Bénédicte Pierru Jérôme Lavergne Béatrice Alonso Monique Sabaty David Pignol |
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Institution: | 1.CEA/Cadarache, DSV/DEVM,Laboratoire de Bioénergétique Cellulaire,France;2.CEA/Valrh?, DSV/DIEP/SBTN,France |
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Abstract: | Background The import of solutes into the bacterial cytoplasm involves several types of membrane transporters, which may be driven by
ATP hydrolysis (ABC transporters) or by an ion or H+ electrochemical membrane potential, as in the tripartite ATP-independent periplasmic system (TRAP). In both the ABC and TRAP
systems, a specific periplasmic protein from the ESR family (Extracytoplasmic Solute Receptors) is often involved for the
recruitment of the solute and its presentation to the membrane complex. In Rhodobacter sphaeroides, TakP (previously named SmoM) is an ESR from a TRAP transporter and binds α-keto acids in vitro. |
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