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| | <StructureSection load='4okk' size='340' side='right'caption='[[4okk]], [[Resolution|resolution]] 2.21Å' scene=''> | | <StructureSection load='4okk' size='340' side='right'caption='[[4okk]], [[Resolution|resolution]] 2.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4okk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OKK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4okk]] 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=4OKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OKK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oke|4oke]], [[4okj|4okj]]</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=4okk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4okk OCA], [https://pdbe.org/4okk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4okk RCSB], [https://www.ebi.ac.uk/pdbsum/4okk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4okk ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv2179c, MT2234.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=4okk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4okk OCA], [http://pdbe.org/4okk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4okk RCSB], [http://www.ebi.ac.uk/pdbsum/4okk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4okk 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Appelmelk, B J]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Berisio, R]] | + | [[Category: Appelmelk BJ]] |
| - | [[Category: Brouwer, F C.C]] | + | [[Category: Berisio R]] |
| - | [[Category: Geurtsen, J J]] | + | [[Category: Brouwer FCC]] |
| - | [[Category: Lacroix, R]] | + | [[Category: Geurtsen JJ]] |
| - | [[Category: Maaskant, J J]] | + | [[Category: Lacroix R]] |
| - | [[Category: Romano, M]] | + | [[Category: Maaskant JJ]] |
| - | [[Category: Roviello, G N]] | + | [[Category: Romano M]] |
| - | [[Category: Sar, A M.van der]] | + | [[Category: Roviello GN]] |
| - | [[Category: Sparrius, M]] | + | [[Category: Sparrius M]] |
| - | [[Category: Stempvoort, G van den Brink-van]] | + | [[Category: Van de Weerd R]] |
| - | [[Category: Weerd, R van de]] | + | [[Category: Van den Brink-van Stempvoort G]] |
| - | [[Category: Alpha/beta fold]]
| + | [[Category: Van der Sar AM]] |
| - | [[Category: Exoribonuclease]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Abendroth J, Ollodart A, Andrews ES, Myler PJ, Staker BL, Edwards TE, Arcus VL, Grundner C. Mycobacterium tuberculosis Rv2179c establishes a new exoribonuclease family with broad phylogenetic distribution. J Biol Chem. 2013 Dec 4. PMID:24311791 doi:http://dx.doi.org/10.1074/jbc.M113.525683
- ↑ 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 and Function of RNase AS, a Polyadenylate-Specific Exoribonuclease Affecting Mycobacterial Virulence In Vivo. Structure. 2014 May 6;22(5):719-30. doi: 10.1016/j.str.2014.01.014. Epub 2014 Apr, 3. PMID:24704253 doi:http://dx.doi.org/10.1016/j.str.2014.01.014
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