Peter, Martin F. 
; Ruland, Jan A. ; Depping, Peer ; Schneberger, Niels ; Severi, Emmanuele ; Moecking, Jonas ; Gatterdam, Karl ; Tindall, Sarah ; Durand, Alexandre ; Heinz, Veronika ; Siebrasse, Jan Peter ; Koenig, Paul-Albert ; Geyer, Matthias ; Ziegler, Christine ; Kubitscheck, Ulrich ; Thomas, Gavin H. ; Hagelueken, Gregor
; Ruland, Jan A. ; Depping, Peer ; Schneberger, Niels ; Severi, Emmanuele ; Moecking, Jonas ; Gatterdam, Karl ; Tindall, Sarah ; Durand, Alexandre ; Heinz, Veronika ; Siebrasse, Jan Peter ; Koenig, Paul-Albert ; Geyer, Matthias ; Ziegler, Christine ; Kubitscheck, Ulrich ; Thomas, Gavin H. ; Hagelueken, Gregor 
Zusammenfassung
Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in bacteria and archaea. Here, the authors used cryo-EM and a range of biophysical techniques to study the structure of function of the sialic acid TRAP transporter HiSiaQM. Tripartite ATP-independent periplasmic (TRAP) transporters are found widely in bacteria and archaea and consist of three structural domains, a soluble ...
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