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| | ==Crystal structure of a putative uncharacterized protein from Mycobacterium tuberculosis== | | ==Crystal structure of a putative uncharacterized protein from Mycobacterium tuberculosis== |
| - | <StructureSection load='4hec' size='340' side='right' caption='[[4hec]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4hec' size='340' side='right'caption='[[4hec]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HEC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEC 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></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT2234.1, Rv2179c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=4hec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hec OCA], [https://pdbe.org/4hec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hec RCSB], [https://www.ebi.ac.uk/pdbsum/4hec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hec ProSAT]</span></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=4hec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hec OCA], [http://pdbe.org/4hec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hec RCSB], [http://www.ebi.ac.uk/pdbsum/4hec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hec ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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 == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Myctu]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Mycobacterium tuberculosis]] | + | |
| - | [[Category: Ssgcid]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| 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
Ribonucleases (RNases) maintain the cellular RNA pool by RNA processing and degradation. In many bacteria including the human pathogen Mycobacterium tuberculosis (Mtb), the enzymes mediating several central RNA processing functions are still unknown. Here, we identify the hypothetical Mtb protein Rv2179c as a highly divergent exoribonuclease. Although the primary sequence of Rv2179c has no detectable similarity to any known RNase, the Rv2179c crystal structure reveals an RNase fold. Active site residues are equivalent to those in the DEDD family of RNases, and Rv2179c has close structural homology to E. coli RNase T. Consistent with the DEDD fold, Rv2179c has exoribonuclease activity, cleaving the 3' single strand overhangs of duplex RNA. Functional orthologs of Rv2179c are prevalent in actinobacteria and found in bacteria as phylogentically distant as proteobacteria. Thus, Rv2179c is the founding member of a new, large RNase family with hundreds of members across the bacterial kingdom.
Mycobacterium tuberculosis Rv2179c establishes a new exoribonuclease family with broad phylogenetic distribution.,Abendroth J, Ollodart A, Andrews ES, Myler PJ, Staker BL, Edwards TE, Arcus VL, Grundner C J Biol Chem. 2013 Dec 4. PMID:24311791[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
- ↑ 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
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