View source for 4x09


==Structure of human RNase 6 in complex with sulphate anions==
<StructureSection load='4x09' size='340' side='right'caption='[[4x09]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4x09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X09 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]] 1.722&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=4x09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x09 OCA], [https://pdbe.org/4x09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x09 RCSB], [https://www.ebi.ac.uk/pdbsum/4x09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x09 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNAS6_HUMAN RNAS6_HUMAN] May have a role in host defense.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human RNase 6 is a cationic secreted protein that belongs to the RNase A superfamily. Its expression is induced in neutrophils and monocytes upon bacterial infection, suggesting a role in host defence. We present here the crystal structure of RNase 6 obtained at a 1.72 A resolution, being the first report for the protein three-dimensional structure and thereby setting the basis for functional studies. The structure shows an overall kidney shaped globular fold shared with the other known family members. Three sulphate anions bound to RNase 6 were found, interacting to residues at the main active site (His15, His122 and Gln14) and cationic surface exposed residues (His36, His39, Arg66 and His67). Kinetic characterization, together with prediction of protein -nucleotide complexes by molecular dynamics, was applied to analyse the RNase 6 substrate nitrogenous base and phosphate selectivity. Our results reveal that, although RNase 6 is a moderate catalyst in comparison to the pancreatic RNase type, its structure includes lineage specific features that facilitate its activity towards polymeric nucleotide substrates. In particular, enzyme interactions at the substrate 5' end can provide an endonuclease type cleavage pattern. Interestingly, the RNase 6 crystal structure revealed a novel secondary active site conformed by the His36-His39 dyad that facilitates the polynucleotide substrate catalysis.

The first crystal structure of human RNase6 reveals a novel substrate binding and cleavage site arrangement.,Prats-Ejarque G, Arranz-Trullen J, Blanco JA, Pulido D, Nogues MV, Moussaoui M, Boix E Biochem J. 2016 Mar 24. pii: BCJ20160245. PMID:27013146<ref>PMID:27013146</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4x09" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arranz-Trullen J]]
[[Category: Blanco JA]]
[[Category: Boix E]]
[[Category: Moussaoui M]]
[[Category: Prats-Ejarque G]]
[[Category: Pulido D]]