3TSR
X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1
Summary for 3TSR
| Entry DOI | 10.2210/pdb3tsr/pdb |
| Descriptor | Ribonuclease pancreatic, Ribonuclease inhibitor, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | hydrolase, hydrolase inhibitor, leucine-rich repeat, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Secreted: P00683 Cytoplasm : Q91VI7 |
| Total number of polymer chains | 8 |
| Total formula weight | 257559.07 |
| Authors | Chang, A.,Lomax, J.E.,Bingman, C.A.,Raines, R.T.,Phillips Jr., G.N. (deposition date: 2011-09-13, release date: 2012-09-19, Last modification date: 2024-10-16) |
| Primary citation | Lomax, J.E.,Bianchetti, C.M.,Chang, A.,Phillips, G.N.,Fox, B.G.,Raines, R.T. Functional evolution of ribonuclease inhibitor: insights from birds and reptiles. J.Mol.Biol., 426:3041-3056, 2014 Cited by PubMed Abstract: Ribonuclease inhibitor (RI) is a conserved protein of the mammalian cytosol. RI binds with high affinity to diverse secretory ribonucleases (RNases) and inhibits their enzymatic activity. Although secretory RNases are found in all vertebrates, the existence of a non-mammalian RI has been uncertain. Here, we report on the identification and characterization of RI homologs from chicken and anole lizard. These proteins bind to RNases from multiple species but exhibit much greater affinity for their cognate RNases than for mammalian RNases. To reveal the basis for this differential affinity, we determined the crystal structure of mouse, bovine, and chicken RI·RNase complexes to a resolution of 2.20, 2.21, and 1.92Å, respectively. A combination of structural, computational, and bioinformatic analyses enabled the identification of two residues that appear to contribute to the differential affinity for RNases. We also found marked differences in oxidative instability between mammalian and non-mammalian RIs, indicating evolution toward greater oxygen sensitivity in RIs from mammalian species. Taken together, our results illuminate the structural and functional evolution of RI, along with its dynamic role in vertebrate biology. PubMed: 24941155DOI: 10.1016/j.jmb.2014.06.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1999 Å) |
Structure validation
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