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4L12

Crystal structure of EGFP-based Calcium Sensor CatchER complexed with Gd

Summary for 4L12
Entry DOI10.2210/pdb4l12/pdb
Related4L13 4L1I
DescriptorEGFP-based Calcium Sensor CatchER, GADOLINIUM ATOM (3 entities in total)
Functional Keywordschromophore, luminescence, fluorescent protein, calcium sensor, metal ions, gadolinium, calcium binding protein
Biological sourceAequorea victoria (Jellyfish)
Total number of polymer chains1
Total formula weight26455.82
Authors
Zhang, Y.,Weber, I.T. (deposition date: 2013-06-01, release date: 2013-12-11, Last modification date: 2024-10-30)
Primary citationZhang, Y.,Reddish, F.,Tang, S.,Zhuo, Y.,Wang, Y.F.,Yang, J.J.,Weber, I.T.
Structural basis for a hand-like site in the calcium sensor CatchER with fast kinetics.
Acta Crystallogr.,Sect.D, 69:2309-2319, 2013
Cited by
PubMed Abstract: Calcium ions, which are important signaling molecules, can be detected in the endoplasmic reticulum by an engineered mutant of green fluorescent protein (GFP) designated CatchER with a fast off-rate. High resolution (1.78-1.20 Å) crystal structures were analyzed for CatchER in the apo form and in complexes with calcium or gadolinium to probe the binding site for metal ions. While CatchER exhibits a 1:1 binding stoichiometry in solution, two positions were observed for each of the metal ions bound within the hand-like site formed by the carboxylate side chains of the mutated residues S147E, S202D, Q204E, F223E and T225E that may be responsible for its fast kinetic properties. Comparison of the structures of CatchER, wild-type GFP and enhanced GFP confirmed that different conformations of Thr203 and Glu222 are associated with the two forms of Tyr66 of the chromophore which are responsible for the absorbance wavelengths of the different proteins. Calcium binding to CatchER may shift the equilibrium for conformational population of the Glu222 side chain and lead to further changes in its optical properties.
PubMed: 24311573
DOI: 10.1107/S0907444913021306
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.78 Å)
Structure validation

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