5xex
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of S.aureus PNPase catalytic domain== | |
| + | <StructureSection load='5xex' size='340' side='right' caption='[[5xex]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xex]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XEX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</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=5xex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xex OCA], [http://pdbe.org/5xex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xex RCSB], [http://www.ebi.ac.uk/pdbsum/5xex PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xex ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PNP_STAA8 PNP_STAA8]] Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.[HAMAP-Rule:MF_01595] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The RNA degradosome of the pathogen Staphylococcus aureus regulates the metabolism of RNA, the expression of virulence factors, and the formation of biofilms. It is composed of the RNases J1/J2, RNase Y, CshA, PNPase, Enolase, Pfk, and a newly identified component, RnpA. However, the function and new partners of RnpA in RNA degradosome remain unknown. Here, we identified PNPase and Enolase as two novel partners for RnpA. Further studies revealed that Enolase interacts with RnpA in competition with PNPase. Enzymatic assays showed that RnpA increases Enolase activity but has no effect on PNPase. These findings provide more information about the functional relationship between RnpA and RNA degradosome. | ||
| - | + | Enolase binds to RnpA in competition with PNPase in Staphylococcus aureus.,Wang X, Wang C, Wu M, Tian T, Cheng T, Zhang X, Zang J FEBS Lett. 2017 Sep 27. doi: 10.1002/1873-3468.12859. PMID:28960276<ref>PMID:28960276</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5xex" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Polyribonucleotide nucleotidyltransferase]] | ||
[[Category: Wang, X]] | [[Category: Wang, X]] | ||
[[Category: Zang, J]] | [[Category: Zang, J]] | ||
| + | [[Category: Zhang, X]] | ||
| + | [[Category: Catalytic domain]] | ||
| + | [[Category: Polynucleotide phosphorylase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:05, 18 October 2017
Crystal structure of S.aureus PNPase catalytic domain
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