Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8

Ekaterina V. Filippova; Karolina L. Tkaczuk; Maksymilian Chruszcz; Xiaohui Xu; Alexei Savchenko; Aled Edwards; Wladek Minor

doi:10.1007/s10969-014-9189-7

Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8

Ekaterina V. Filippova, Karolina L. Tkaczuk, Maksymilian Chruszcz, Xiaohui Xu, Alexei Savchenko, Aled Edwards, Wladek Minor^*

^*Corresponding author for this work

Biochemistry and Molecular Genetics

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	215-222
Number of pages	8
Journal	Journal of Structural and Functional Genomics
Volume	15
Issue number	4
DOIs	https://doi.org/10.1007/s10969-014-9189-7
State	Published - Nov 20 2014

Funding

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.

Keywords

Nucleotide binding domain structure
Putative ABC-type transporter
Putative NatAB permease
Thermotoga maritima

ASJC Scopus subject areas

Genetics
Structural Biology
Biochemistry

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10.1007/s10969-014-9189-7

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title = "Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8",

abstract = "This study describes the structure of the putative ABC-type 2 transporter TM0543 from Thermotoga maritimaMSB8 determined at a resolution of 2.3 {\AA}. 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.",

keywords = "Nucleotide binding domain structure, Putative ABC-type transporter, Putative NatAB permease, Thermotoga maritima",

author = "Filippova, {Ekaterina V.} and Tkaczuk, {Karolina L.} and Maksymilian Chruszcz and Xiaohui Xu and Alexei Savchenko and Aled Edwards and Wladek Minor",

note = "Publisher Copyright: {\textcopyright} 2014, Springer Science+Business Media Dordrecht.",

year = "2014",

month = nov,

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doi = "10.1007/s10969-014-9189-7",

language = "English (US)",

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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

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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Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8

Abstract

Funding

Keywords

ASJC Scopus subject areas

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Crystal structure of a domain of a putative ABC type-2 transporter from Thermotoga maritima MSB8

Cite this

Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8

Abstract

Funding

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Datasets

Crystal structure of a domain of a putative ABC type-2 transporter from Thermotoga maritima MSB8

Cite this