|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of the polynucleotide phosphorylase (CBU_0852) from Coxiella burnetii== | | ==Structure of the polynucleotide phosphorylase (CBU_0852) from Coxiella burnetii== |
| - | <StructureSection load='4nbq' size='340' side='right' caption='[[4nbq]], [[Resolution|resolution]] 2.91Å' scene=''> | + | <StructureSection load='4nbq' size='340' side='right'caption='[[4nbq]], [[Resolution|resolution]] 2.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nbq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Coxbu Coxbu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NBQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nbq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxiella_burnetii_RSA_493 Coxiella burnetii RSA 493]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NBQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4nbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nbq OCA], [https://pdbe.org/4nbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nbq RCSB], [https://www.ebi.ac.uk/pdbsum/4nbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nbq ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pnp, CBU_0852 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227377 COXBU])</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=4nbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nbq OCA], [http://pdbe.org/4nbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nbq RCSB], [http://www.ebi.ac.uk/pdbsum/4nbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nbq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PNP_COXBU PNP_COXBU]] Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | + | [https://www.uniprot.org/uniprot/PNP_COXBU PNP_COXBU] Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 4nbq" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4nbq" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Coxbu]] | + | [[Category: Coxiella burnetii RSA 493]] |
| - | [[Category: Polyribonucleotide nucleotidyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Burshteyn, F]] | + | [[Category: Burshteyn F]] |
| - | [[Category: Cassidy, M]] | + | [[Category: Cassidy M]] |
| - | [[Category: Cheung, J]] | + | [[Category: Cheung J]] |
| - | [[Category: Franklin, M C]] | + | [[Category: Franklin MC]] |
| - | [[Category: Gary, E]] | + | [[Category: Gary E]] |
| - | [[Category: Love, J]] | + | [[Category: Love J]] |
| - | [[Category: Rudolph, M J]] | + | [[Category: Rudolph MJ]] |
| - | [[Category: Phosphorylase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PNP_COXBU Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Publication Abstract from PubMed
Coxiella burnetii is a highly infectious bacterium and potential agent of bioterrorism. However, it has not been studied as extensively as other biological agents, and very few of its proteins have been structurally characterized. To address this situation, we undertook a study of critical metabolic enzymes in C. burnetii that have great potential as drug targets. We used high-throughput techniques to produce novel crystal structures of 48 of these proteins. We selected one protein, C. burnetii dihydrofolate reductase (CbDHFR), for additional work to demonstrate the value of these structures for structure-based drug design. This enzyme's structure reveals a feature in the substrate binding groove that is different between CbDHFR and human dihydrofolate reductase (hDFHR). We then identified a compound by in silico screening that exploits this binding groove difference, and demonstrated that this compound inhibits CbDHFR with at least 25-fold greater potency than hDHFR. Since this binding groove feature is shared by many other prokaryotes, the compound identified could form the basis of a novel antibacterial agent effective against a broad spectrum of pathogenic bacteria. This article is protected by copyright. All rights reserved.
Structural Genomics for Drug Design against the Pathogen Coxiella burnetii.,Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD Proteins. 2015 Jun 1. doi: 10.1002/prot.24841. PMID:26033498[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD. Structural Genomics for Drug Design against the Pathogen Coxiella burnetii. Proteins. 2015 Jun 1. doi: 10.1002/prot.24841. PMID:26033498 doi:http://dx.doi.org/10.1002/prot.24841
|
