TY - JOUR
T1 - Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8
AU - Filippova, Ekaterina V.
AU - Tkaczuk, Karolina L.
AU - Chruszcz, Maksymilian
AU - Xu, Xiaohui
AU - Savchenko, Alexei
AU - Edwards, Aled
AU - Minor, Wladek
N1 - Funding Information:
Acknowledgments The work described in this paper was supported by NIH PSI Grants GM74492 and GM094585. The results shown in this report are derived from work performed at Argonne National Laboratory, at the Structural Biology Center of the Advanced Photon Source. Argonne is operated by University of Chicago Argonne, LLC, for the U.S. Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. We would also like to thank Dr Matthew D. Zimmerman for critically reading and correcting the manuscript.
Publisher Copyright:
© 2014, Springer Science+Business Media Dordrecht.
PY - 2014/11/20
Y1 - 2014/11/20
N2 - This study describes the structure of the putative ABC-type 2 transporter TM0543 from Thermotoga maritimaMSB8 determined at a resolution of 2.3 Å. In comparative sequence-clustering analysis, TM0543 displays similarity to NatAB-like proteins, which are components of the ABC-type Na+ efflux pump permease. However, the overall structure fold of the predicted nucleotide-binding domain reveals that it is different from any known structure of ABC-type efflux transporters solved to date. The structure of the putative TM0543 domain also exhibits different dimer architecture and topology of its presumed ATP binding pocket, which may indicate that it does not bind nucleotide at all. Structural analysis of calcium ion binding sites found at the interface between TM0543 dimer subunits suggests that protein may be involved in ion-transporting activity. A detailed analysis of the protein sequence and structure is presented and discussed.
AB - This study describes the structure of the putative ABC-type 2 transporter TM0543 from Thermotoga maritimaMSB8 determined at a resolution of 2.3 Å. In comparative sequence-clustering analysis, TM0543 displays similarity to NatAB-like proteins, which are components of the ABC-type Na+ efflux pump permease. However, the overall structure fold of the predicted nucleotide-binding domain reveals that it is different from any known structure of ABC-type efflux transporters solved to date. The structure of the putative TM0543 domain also exhibits different dimer architecture and topology of its presumed ATP binding pocket, which may indicate that it does not bind nucleotide at all. Structural analysis of calcium ion binding sites found at the interface between TM0543 dimer subunits suggests that protein may be involved in ion-transporting activity. A detailed analysis of the protein sequence and structure is presented and discussed.
KW - Nucleotide binding domain structure
KW - Putative ABC-type transporter
KW - Putative NatAB permease
KW - Thermotoga maritima
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U2 - 10.1007/s10969-014-9189-7
DO - 10.1007/s10969-014-9189-7
M3 - Article
C2 - 25306867
AN - SCOPUS:84911959945
SN - 1345-711X
VL - 15
SP - 215
EP - 222
JO - Journal of Structural and Functional Genomics
JF - Journal of Structural and Functional Genomics
IS - 4
ER -