Title |
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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Published in |
BMC Molecular and Cell Biology, March 2007
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DOI | 10.1186/1472-6807-7-11 |
Pubmed ID | |
Authors |
Sophie Gonin, Pascal Arnoux, Bénédicte Pierru, Jérôme Lavergne, Béatrice Alonso, Monique Sabaty, David Pignol |
Abstract |
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 alpha-keto acids in vitro. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 2% |
Portugal | 1 | 2% |
Unknown | 47 | 96% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 10 | 20% |
Researcher | 10 | 20% |
Student > Bachelor | 6 | 12% |
Student > Master | 4 | 8% |
Student > Doctoral Student | 3 | 6% |
Other | 9 | 18% |
Unknown | 7 | 14% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 21 | 43% |
Biochemistry, Genetics and Molecular Biology | 15 | 31% |
Chemistry | 3 | 6% |
Immunology and Microbiology | 1 | 2% |
Design | 1 | 2% |
Other | 0 | 0% |
Unknown | 8 | 16% |