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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 390, Issue 11

Issues

Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation

Christine Oswald
  • Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, D-40225 Düsseldorf, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Sander H.J. Smits
  • Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, D-40225 Düsseldorf, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Marina Höing
  • Laboratory for Microbiology, Department of Biology, Philipps University Marburg, Karl-von-Frisch Str. 8, D-35032 Marburg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Erhard Bremer
  • Laboratory for Microbiology, Department of Biology, Philipps University Marburg, Karl-von-Frisch Str. 8, D-35032 Marburg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Lutz Schmitt
  • Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, D-40225 Düsseldorf, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2009-07-30 | DOI: https://doi.org/10.1515/BC.2009.113

Abstract

The periplasmic ligand-binding protein ChoX is part of the ABC transport system ChoVWX that imports choline as a nutrient into the soil bacterium Sinorhizobium meliloti. We have recently reported the crystal structures of ChoX in complex with its ligands choline and acetylcholine and the structure of a fully closed but substrate-free state of ChoX. This latter structure revealed an architecture of the ligand-binding site that is superimposable to the closed, ligand-bound form of ChoX. We report here the crystal structure of ChoX in an unusual, ligand-free conformation that represents a semi-closed form of ChoX. The analysis revealed a subdomain movement in the N-lobe of ChoX. Comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.

Keywords: ABC transporter; choline-binding protein; conformational change; membrane transport

About the article

Corresponding author


Received: 2009-05-13

Accepted: 2009-06-05

Published Online: 2009-07-30

Published in Print: 2009-11-01


Citation Information: Biological Chemistry, Volume 390, Issue 11, Pages 1163–1170, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.113.

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