9ftw | pdb_00009ftw

Crystal structure of calcium-activated EndoU

spinqualitylabelsall models 9ftw, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ftw is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ENDOU_HUMAN Endoribonuclease that cleaves single-stranded RNAs at 5' of uridylates and releases a product with a 2',3'-cyclic phosphate at the 3'-end. The UU and GU sites are more efficiently cleaved than CU and AU sites. Publication Abstract from PubMed Ribonucleases (RNases) are ubiquitous enzymes that process or degrade RNA, essential for cellular functions and immune responses. The EndoU-like superfamily includes endoribonucleases conserved across bacteria, eukaryotes, and certain viruses, with an ancient evolutionary link to the ribonuclease A-like superfamily. Both bacterial EndoU and animal RNase A share a similar fold and function independently of cofactors. In contrast, the eukaryotic EndoU catalytic domain requires divalent metal ions for catalysis, possibly due to an N-terminal extension near the catalytic core. In this study, we used biophysical and computational techniques along with in vitro assays to investigate the calcium-dependent activation of human EndoU. We determined the crystal structure of EndoU bound to calcium and found that calcium binding remote from the catalytic triad triggers water-mediated intramolecular signaling and structural changes, activating the enzyme through allostery. Calcium-binding involves residues from both the catalytic core and the N-terminal extension, indicating that the N-terminal extension interacts with the catalytic core to modulate activity in response to calcium. Our findings suggest that similar mechanisms may be present across all eukaryotic EndoUs, highlighting a unique evolutionary adaptation that connects endoribonuclease activity to cellular signaling in eukaryotes. Molecular Basis for the Calcium-Dependent Activation of the Ribonuclease EndoU.,Malard F, Dias K, Baudy M, Thore S, Vialet B, Barthelemy P, Fribourg S, Karginov FV, Campagne S Res Sq [Preprint]. 2024 Jul 15:rs.3.rs-4654759. doi: 10.21203/rs.3.rs-4654759/v1. PMID:39070628 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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