3tsr: Difference between revisions
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==X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1== | |||
<StructureSection load='3tsr' size='340' side='right'caption='[[3tsr]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tsr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TSR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1999Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsr OCA], [https://pdbe.org/3tsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tsr RCSB], [https://www.ebi.ac.uk/pdbsum/3tsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RNAS1_MOUSE RNAS1_MOUSE] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 1.92A, 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. | |||
Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles.,Lomax JE, Bianchetti CM, Chang A, Phillips GN Jr, Fox BG, Raines RT J Mol Biol. 2014 Jun 15. pii: S0022-2836(14)00287-3. doi:, 10.1016/j.jmb.2014.06.007. PMID:24941155<ref>PMID:24941155</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3tsr" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
*[[Ribonuclease inhibitor|Ribonuclease inhibitor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Bingman CA]] | |||
[[Category: Bingman | [[Category: Chang A]] | ||
[[Category: Chang | [[Category: Lomax JE]] | ||
[[Category: Lomax | [[Category: Phillips Jr GN]] | ||
[[Category: Phillips | [[Category: Raines RT]] | ||
[[Category: Raines | |||
Latest revision as of 09:12, 17 October 2024
X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1
Structural highlights
FunctionRNAS1_MOUSE Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). Publication Abstract from PubMedRibonuclease 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 1.92A, 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. Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles.,Lomax JE, Bianchetti CM, Chang A, Phillips GN Jr, Fox BG, Raines RT J Mol Biol. 2014 Jun 15. pii: S0022-2836(14)00287-3. doi:, 10.1016/j.jmb.2014.06.007. PMID:24941155[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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