7bfk: Difference between revisions
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==X-ray structure of SS-RNase-2== | ==X-ray structure of SS-RNase-2== | ||
<StructureSection load='7bfk' size='340' side='right'caption='[[7bfk]]' scene=''> | <StructureSection load='7bfk' size='340' side='right'caption='[[7bfk]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BFK FirstGlance]. <br> | <table><tr><td colspan='2'>[[7bfk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BFK FirstGlance]. <br> | ||
</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=7bfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bfk OCA], [https://pdbe.org/7bfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bfk RCSB], [https://www.ebi.ac.uk/pdbsum/7bfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bfk ProSAT]</span></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7bfl|7bfl]]</div></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=7bfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bfk OCA], [https://pdbe.org/7bfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bfk RCSB], [https://www.ebi.ac.uk/pdbsum/7bfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bfk ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:33848550</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7bfk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Krauss, I Russo]] | ||
[[Category: Sica F]] | [[Category: Sica, F]] | ||
[[Category: Troisi R]] | [[Category: Troisi, R]] | ||
[[Category: Ancient ribonuclease]] | |||
[[Category: Auto-inhibition]] | |||
[[Category: Hydrolase]] | |||
[[Category: Rnase]] | |||
[[Category: Salmo salar]] | |||
Revision as of 12:07, 5 May 2021
X-ray structure of SS-RNase-2X-ray structure of SS-RNase-2
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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