4oke: Difference between revisions
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''' | ==Structure of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo== | ||
<StructureSection load='4oke' size='340' side='right' caption='[[4oke]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== 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> | |||
</td></tr><tr><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><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4okj|4okj]], [[4okk|4okk]]</td></tr> | |||
<tr><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> | |||
<table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Berisio, R.]] | |||
[[Category: Romano, M.]] | |||
[[Category: Capsular polysaccharide]] | |||
[[Category: Hydrolase]] | |||
[[Category: M. tuberculosis]] | |||
[[Category: Ribonuclease]] | |||
[[Category: Virulence]] | |||
Revision as of 09:05, 21 May 2014
Structure of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo
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