6d1r
From Proteopedia
(Difference between revisions)
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<StructureSection load='6d1r' size='340' side='right' caption='[[6d1r]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6d1r' size='340' side='right' caption='[[6d1r]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6d1r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D1R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d1r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D1R FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] </span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] </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=6d1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d1r OCA], [http://pdbe.org/6d1r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d1r RCSB], [http://www.ebi.ac.uk/pdbsum/6d1r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d1r 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=6d1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d1r OCA], [http://pdbe.org/6d1r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d1r RCSB], [http://www.ebi.ac.uk/pdbsum/6d1r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d1r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RNPA_STAAU RNPA_STAAU]] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | [[http://www.uniprot.org/uniprot/RNPA_STAAU RNPA_STAAU]] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein component for two essential cellular processes, RNA degradation and transfer-RNA (tRNA) maturation. The first crystal structure of RnpA from the pathogenic bacterial species, S. aureus, is reported at 2.0 A resolution. The structure presented maintains key similarities with previously reported RnpA structures from bacteria and archaea, including the highly conserved RNR-box region and aromatic residues in the precursor-tRNA 5'-leader-binding domain. This structure will be instrumental in the pursuit of structure-based designed inhibitors targeting RnpA-mediated RNA processing as a novel therapeutic approach for treating S. aureus infections. | ||
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| + | Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus.,Ha L, Colquhoun J, Noinaj N, Das C, Dunman PM, Flaherty DP Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):632-637. doi:, 10.1107/S2053230X18011512. Epub 2018 Sep 19. PMID:30279314<ref>PMID:30279314</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6d1r" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ribonuclease|Ribonuclease]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:35, 17 October 2018
Structure of Staphylococcus aureus RNase P protein at 2.0 angstrom
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Categories: Ribonuclease P | Colquhoun, J | Das, C | Dunman, P | Flaherty, D P | Ha, L | Noinaj, N | P protein | Rna binding protein | Rna metabolism | Rnase | Trna processing
