7bfl | pdb_00007bfl

X-ray structure of SS-RNase-2 des116-120

spinqualitylabelsall models 7bfl, resolution 2.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.88Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The superfamily of vertebrate ribonucleases, a large group of evolutionarily related proteins, continues to provide interesting structural and functional information. In particular, the crystal structure of SS-RNase-2 from Salmo salar (SS2), here presented, has revealed a novel auto-inhibition mechanism that enriches the number of inhibition strategies observed in some members of the family. Within an essentially unmodified RNase folding, the SS2 active site cleft is in part obstructed by the collapse of an extra pentapeptide inserted in the C-terminal region. This unexpected intrusion alters the organization of the catalytic triad by pushing one catalytic histidine off the pocket. Possible mechanisms to remove the active site obstruction have also been studied through the production of two mutants that provide useful information on the functionality of this intriguing version of the ribonuclease superfamily. The structural features of an ancient ribonuclease from Salmo salar reveal an intriguing case of auto-inhibition.,Sica F, Russo Krauss I, Troisi R, Bosso A, Culurciello R, Carluccio C, Trapani M, Merlino A, Mazzarella L, Pizzo E Int J Biol Macromol. 2021 Apr 15;182:659-668. doi:, 10.1016/j.ijbiomac.2021.04.041. PMID:33848550 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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