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==The X-ray structure of zebrafish RNase1 from a new crystal form at pH 4.5== | ==The X-ray structure of zebrafish RNase1 from a new crystal form at pH 4.5== | ||
<StructureSection load='3ljd' size='340' side='right' caption='[[3ljd]], [[Resolution|resolution]] 1.38Å' scene=''> | <StructureSection load='3ljd' size='340' side='right'caption='[[3ljd]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ljd]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ljd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LJD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ljd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ljd OCA], [https://pdbe.org/3ljd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ljd RCSB], [https://www.ebi.ac.uk/pdbsum/3ljd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ljd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/E7FH76_DANRE E7FH76_DANRE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 3ljd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3ljd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Danio rerio]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Mazzarella | [[Category: Mazzarella L]] | ||
[[Category: Merlino | [[Category: Merlino A]] | ||
[[Category: | [[Category: Russo Krauss I]] | ||
[[Category: | [[Category: Sica F]] | ||
Latest revision as of 11:38, 6 September 2023
The X-ray structure of zebrafish RNase1 from a new crystal form at pH 4.5The X-ray structure of zebrafish RNase1 from a new crystal form at pH 4.5
Structural highlights
FunctionPublication Abstract from PubMedOnly recently extracellular RNases of the RNase A superfamily, with the characteristic CKxxNTF sequence signature, have been identified in fish. This has led to the recognition that these RNases are present in the whole vertebrate sub-phylum. In fact, they comprise the only enzyme family unique to vertebrates. Four RNases from zebrafish (Danio rerio) have been previously reported, with a very low RNase activity, some endowed, like human angiogenin, with powerful angiogenic and bactericidal activities. Here we report the three-dimensional structure, the thermodynamic behaviour, and the biological properties of a novel zebrafish RNase, ZF-RNase-5. The investigation of its structural and functional properties, extended to all other sub-family members, provides an inclusive description of the whole zebrafish RNase sub-family. A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish.,Pizzo E, Merlino A, Turano M, Russo Krauss I, Coscia F, Zanfardino A, Varcamonti M, Furia A, Giancola C, Mazzarella L, Sica F, D'Alessio G Biochem J. 2010 Nov 4. PMID:21050179[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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