7bfl

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(New page: '''Unreleased structure''' The entry 7bfl is ON HOLD until Paper Publication Authors: Sica, F., Russo Krauss, I., Troisi, R. Description: X-ray structure of SS-RNase-2 des116-120 [[Cat...)
Current revision (06:07, 21 November 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 7bfl is ON HOLD until Paper Publication
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==X-ray structure of SS-RNase-2 des116-120==
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<StructureSection load='7bfl' size='340' side='right'caption='[[7bfl]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BFL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.88&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7bfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bfl OCA], [https://pdbe.org/7bfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bfl RCSB], [https://www.ebi.ac.uk/pdbsum/7bfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bfl ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Sica, F., Russo Krauss, I., Troisi, R.
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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>
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Description: X-ray structure of SS-RNase-2 des116-120
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Troisi, R]]
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<div class="pdbe-citations 7bfl" style="background-color:#fffaf0;"></div>
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[[Category: Russo Krauss, I]]
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[[Category: Sica, F]]
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Russo Krauss I]]
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[[Category: Sica F]]
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[[Category: Troisi R]]

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

PDB ID 7bfl

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