4ttg

Beta-galactosidase (E. coli) in the presence of potassium chloride.

spinqualitylabelsall models 4ttg, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ttg is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CL, CSD, DMS, K, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BGAL_ECOLX Publication Abstract from PubMed Many enzymes require a specific monovalent cation (M(+)), that is either Na(+) or K(+), for optimal activity. While high selectivity M(+) sites in transport proteins have been extensively studied, enzyme M(+) binding sites generally have lower selectivity and are less characterized. Here we study the M(+) binding site of the model enzyme E. coli beta-galactosidase, which is about 10 fold selective for Na(+) over K(+). Combining data from X-ray crystallography and computational models, we find the electrostatic environment predominates in defining the Na(+) selectivity. In this lower selectivity site rather subtle influences on the electrostatic environment become significant, including the induced polarization effects of the M(+) on the coordinating ligands and the effect of second coordination shell residues on the charge distribution of the primary ligands. This work expands the knowledge of ion selectivity in proteins to denote novel mechanisms important for the selectivity of M(+) sites in enzymes. Elucidating factors important for monovalent cation selectivity in enzymes: E. coli beta-galactosidase as a model.,Wheatley RW, Juers DH, Lev BB, Huber RE, Noskov SY Phys Chem Chem Phys. 2015 Apr 8;17(16):10899-909. doi: 10.1039/c4cp04952g. PMID:25820412 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactosidase 3D structures

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