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==Structure of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo==
==Structure of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo==
<StructureSection load='4oke' size='340' side='right' caption='[[4oke]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4oke' size='340' side='right'caption='[[4oke]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4oke]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OKE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4oke]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OKE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4okj|4okj]], [[4okk|4okk]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oke OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oke RCSB], [http://www.ebi.ac.uk/pdbsum/4oke PDBsum]</span></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=4oke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oke OCA], [https://pdbe.org/4oke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oke RCSB], [https://www.ebi.ac.uk/pdbsum/4oke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oke ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EXRBN_MYCTU EXRBN_MYCTU]] Exonuclease that cleaves single-stranded 3' overhangs of double-stranded RNA. Has no activity with 5' overhangs. Has negligible endonuclease activity. Can bind ATP, dATP and AMP (in vitro); the nucleotide occupies the predicted substrate binding site.<ref>PMID:24311791</ref> 
[https://www.uniprot.org/uniprot/EXRBN_MYCTU EXRBN_MYCTU] Exonuclease that cleaves single-stranded 3' overhangs of double-stranded RNA. Has no activity with 5' overhangs. Has negligible endonuclease activity. Can bind ATP, dATP and AMP (in vitro); the nucleotide occupies the predicted substrate binding site.<ref>PMID:24311791</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cell-envelope of Mycobacterium tuberculosis plays a key role in bacterial virulence and antibiotic resistance. Little is known about the molecular mechanisms of regulation of cell-envelope formation. Here, we elucidate functional and structural properties of RNase AS, which modulates M. tuberculosis cell-envelope properties and strongly impacts bacterial virulence in vivo. The structure of RNase AS reveals a resemblance to RNase T from Escherichia coli, an RNase of the DEDD family involved in RNA maturation. We show that RNase AS acts as a 3'-5'-exoribonuclease that specifically hydrolyzes adenylate-containing RNA sequences. Also, crystal structures of complexes with AMP and UMP reveal the structural basis for the observed enzyme specificity. Notably, RNase AS shows a mechanism of substrate recruitment, based on the recognition of the hydrogen bond donor NH2 group of adenine. Our work opens a field for the design of drugs able to reduce bacterial virulence in vivo.
 
Structure and Function of RNase AS, a Polyadenylate-Specific Exoribonuclease Affecting Mycobacterial Virulence In Vivo.,Romano M, van de Weerd R, Brouwer FC, Roviello GN, Lacroix R, Sparrius M, van den Brink-van Stempvoort G, Maaskant JJ, van der Sar AM, Appelmelk BJ, Geurtsen JJ, Berisio R Structure. 2014 May 6;22(5):719-30. doi: 10.1016/j.str.2014.01.014. Epub 2014 Apr, 3. PMID:24704253<ref>PMID:24704253</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Berisio, R]]
[[Category: Large Structures]]
[[Category: Romano, M]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Capsular polysaccharide]]
[[Category: Berisio R]]
[[Category: Hydrolase]]
[[Category: Romano M]]
[[Category: M. tuberculosis]]
[[Category: Ribonuclease]]
[[Category: Virulence]]
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