3hcq

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

Structural highlights

3hcq is a 2 chain structure with sequence from Sinorhizobium meliloti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.89Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q92N37_RHIME

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation.,Oswald C, Smits SH, Hoing M, Bremer E, Schmitt L Biol Chem. 2009 Nov;390(11):1163-70. PMID:19642870[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. Oswald C, Smits SH, Hoing M, Bremer E, Schmitt L. Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation. Biol Chem. 2009 Nov;390(11):1163-70. PMID:19642870 doi:10.1515/BC.2009.113

Contents


PDB ID 3hcq

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