1b8l

Calcium-bound D51A/E101D/F102W Triple Mutant of Beta Carp ParvalbuminCalcium-bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin

Structural highlights 1b8l is a 1 chain structure with sequence from Cyprinus carpio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRVB_CYPCA In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. 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 BACKGROUND: The EF-hand family is a large set of Ca(2+)-binding proteins that contain characteristic helix-loop-helix binding motifs that are highly conserved in sequence. Members of this family include parvalbumin and many prominent regulatory proteins such as calmodulin and troponin C. EF-hand proteins are involved in a variety of physiological processes including cell-cycle regulation, second messenger production, muscle contraction, microtubule organization and vision. RESULTS: We have determined the structures of parvalbumin mutants designed to explore the role of the last coordinating residue of the Ca(2+)-binding loop. An E101D substitution has been made in the parvalbumin EF site. The substitution decreases the Ca(2+)-binding affinity 100-fold and increases the Mg(2+)-binding affinity 10-fold. Both the Ca(2+)- and Mg(2+)-bound structures have been determined, and a structural basis has been proposed for the metal-ion-binding properties. CONCLUSIONS: The E101D mutation does not affect the Mg(2+) coordination geometry of the binding loop, but it does pull the F helix 1.1 A towards the loop. The E101D-Ca(2+) structure reveals that this mutant cannot obtain the sevenfold coordination preferred by Ca(2+), presumably because of strain limits imposed by tertiary structure. Analysis of these results relative to previously reported structural information supports a model wherein the characteristics of the last coordinating residue and the plasticity of the Ca(2+)-binding loop delimit the allowable geometries for the coordinating sphere. Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin.,Cates MS, Berry MB, Ho EL, Li Q, Potter JD, Phillips GN Jr Structure. 1999 Oct 15;7(10):1269-78. PMID:10545326 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Parvalbumin

spinqualitylabelsall models 1b8l, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image