5yjj
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of PNPase from Staphylococcus epidermidis== | |
| + | <StructureSection load='5yjj' size='340' side='right' caption='[[5yjj]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5yjj]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YJJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YJJ 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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polyribonucleotide_nucleotidyltransferase Polyribonucleotide nucleotidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.8 2.7.7.8] </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=5yjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yjj OCA], [http://pdbe.org/5yjj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yjj RCSB], [http://www.ebi.ac.uk/pdbsum/5yjj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yjj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PNP_STAES PNP_STAES]] Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polynucleotide phosphorylase catalyzes both 3'-5' exoribonuclease and polyadenylation reactions. The crystal structure of Staphylococcus epidermidis PNPase revealed a bound phosphate in the PH2 domain of each protomer coordinated by three adjacent serine residues. Mutational analysis suggests that phosphate coordination by these serine residues is essential to maintain the catalytic center in an active conformation. We note that PNPase forms a complex with RNase J1 and RNase J2 without substantially altering either exo-ribonuclease or polyadenylation activity of this enzyme. This decoupling of catalytic activity from protein-protein interactions suggests that association of these endo- or exo-ribonucleases with PNPase could be more relevant for cellular localization or concerted targeting of structured RNA for recycling. | ||
| - | + | Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2.,Raj R, Mitra S, Gopal B Biochem Biophys Res Commun. 2018 Jan 8;495(2):2078-2084. doi:, 10.1016/j.bbrc.2017.12.056. Epub 2017 Dec 11. PMID:29242153<ref>PMID:29242153</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5yjj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Polyribonucleotide nucleotidyltransferase]] | ||
[[Category: Gopal, B]] | [[Category: Gopal, B]] | ||
[[Category: Raj, R]] | [[Category: Raj, R]] | ||
| + | [[Category: Cytosolic protein]] | ||
| + | [[Category: Polyadenylation]] | ||
| + | [[Category: Polynucleotidyl phosphorylase]] | ||
| + | [[Category: Rna degradation]] | ||
Revision as of 05:54, 31 January 2018
Crystal structure of PNPase from Staphylococcus epidermidis
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