9u9d

Bipartite Genetically Encoded Biosensor sG-GECO1

spinqualitylabelsall models 9u9d, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9u9d is a 2 chain structure with sequence from Aequorea victoria, Gallus gallus, Rattus norvegicus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CRO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CALM1_RAT Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]MYLK_CHICK Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals.GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. Publication Abstract from PubMed Self-complementing bipartite fluorescent proteins (FPs) are useful tools for the detection of protein-protein proximity and for localizing fluorophores to membrane-membrane contact sites. Here, we report versions of circularly permuted green FP (GFP), red FP (RFP), and mNeonGreen (NG), which are split into a large fragment composed of nine beta-strands and a small fragment composed of two beta-strands. In each case, the large and small fragments can associate in live cells to form the complete 11-stranded FP beta-barrel. We further converted each of these three self-complementing FPs into bipartite calcium ion (Ca(2+)) biosensors. We demonstrate that appropriately targeted versions of these split FPs, and split FP-based biosensors, can be functionally assembled at membrane-membrane contact sites. We employ the bipartite NG-based Ca(2+) biosensor for visualization of pharmacologically induced Ca(2+) release at mitochondria-endoplasmic reticulum contact sites (MERCs). Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites.,Yamaguchi I, Barazzuol L, Dematteis G, Zhu W, Wen Y, Drobizhev M, Lim D, Campbell RE, Cali T, Nasu Y Anal Chem. 2025 Sep 16;97(36):19848-19861. doi: 10.1021/acs.analchem.5c03831. , Epub 2025 Sep 1. PMID:40888292 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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