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Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation
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Christine Oswald
Published/Copyright:
July 30, 2009
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.
Received: 2009-5-13
Accepted: 2009-6-5
Published Online: 2009-07-30
Published in Print: 2009-11-01
©2009 by Walter de Gruyter Berlin New York
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Keywords for this article
ABC transporter;
choline-binding protein;
conformational change;
membrane transport
Articles in the same Issue
- Editorial
- Highlight: Molecular and Cellular Mechanisms of Memory
- Highlight: 60th Mosbach Colloquium of the GBM ‘Molecular and Cellular Mechanisms of Memory’
- Protein carboxyl methylation and the biochemistry of memory
- Chemotaxis: how bacteria use memory
- Mechanistic insights in light-induced cAMP production by photoactivated adenylyl cyclase alpha (PACα)
- Balance of power – dynamic regulation of chromatin in plant development
- Ultrafast memory loss and relaxation processes in hydrogen-bonded systems
- Memory and neural networks on the basis of color centers in solids
- Dissection of gene regulatory networks in embryonic stem cells by means of high-throughput sequencing
- The epigenetic bottleneck of neurodegenerative and psychiatric diseases
- Protein Structure and Function
- Mechanism of activation of Saccharomyces cerevisiae calcineurin by Mn2+
- Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation
- Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg257/Lys260, and unmasking of acid-base catalysis
- Genes and Nucleic Acids
- CA/C1 peptidases of the malaria parasites Plasmodium falciparum and P. berghei and their mammalian hosts – a bioinformatical analysis
- Proteolysis
- Placental expression of proteases and their inhibitors in patients with HELLP syndrome
- Irreversible inhibition of human cathepsins B, L, S and K by hypervalent tellurium compounds
