3hcq | pdb_00003hcq

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

spinqualitylabelsall models 3hcq, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Related: 2reg, 2rin Gene: choX, R02399, SMc02737 (Sinorhizobium meliloti) Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter

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