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| | ==Crystal Structure of P. aeruginosa peptidyl-tRNA hydrolase== | | ==Crystal Structure of P. aeruginosa peptidyl-tRNA hydrolase== |
| - | <StructureSection load='4fyj' size='340' side='right' caption='[[4fyj]], [[Resolution|resolution]] 1.77Å' scene=''> | + | <StructureSection load='4fyj' size='340' side='right'caption='[[4fyj]], [[Resolution|resolution]] 1.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fyj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fyj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYJ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pth, PA4672 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr> | + | </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=4fyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyj OCA], [https://pdbe.org/4fyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fyj RCSB], [https://www.ebi.ac.uk/pdbsum/4fyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyj ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] </span></td></tr>
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| - | <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=4fyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyj OCA], [http://pdbe.org/4fyj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fyj RCSB], [http://www.ebi.ac.uk/pdbsum/4fyj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PTH_PSEAE PTH_PSEAE]] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). | + | [https://www.uniprot.org/uniprot/PTH_PSEAE PTH_PSEAE] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4fyj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4fyj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aminoacyl-tRNA hydrolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Hughes, R C]] | + | [[Category: Hughes RC]] |
| - | [[Category: McFeeters, H]] | + | [[Category: McFeeters H]] |
| - | [[Category: McFeeters, R L]] | + | [[Category: McFeeters RL]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
PTH_PSEAE The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).
Publication Abstract from PubMed
The peptidyl-tRNA hydrolase enzyme from the pathogenic bacterium Pseudomonas aeruginosa (Pth; EC 3.1.1.29) has been cloned, expressed in Escherichia coli and crystallized for X-ray structural analysis. Suitable crystals were grown using the sitting-drop vapour-diffusion method after one week of incubation against a reservoir solution consisting of 20% polyethylene glycol 4000, 100 mM Tris pH 7.5, 10%(v/v) isopropyl alcohol. The crystals were used to obtain the three-dimensional structure of the native protein at 1.77 A resolution. The structure was determined by molecular replacement of the crystallographic data processed in space group P6(1)22 with unit-cell parameters a = b = 63.62, c = 155.20 A, alpha = beta = 90, gamma = 120 degrees . The asymmetric unit of the crystallographic lattice was composed of a single copy of the enzyme molecule with a 43% solvent fraction, corresponding to a Matthews coefficient of 2.43 A(3) Da(-1). The crystallographic structure reported here will serve as the foundation for future structure-guided efforts towards the development of novel small-molecule inhibitors specific to bacterial Pths.
Recombinant production, crystallization and X-ray crystallographic structure determination of the peptidyl-tRNA hydrolase of Pseudomonas aeruginosa.,Hughes RC, McFeeters H, Coates L, McFeeters RL Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1472-6., doi: 10.1107/S1744309112045770. Epub 2012 Nov 28. PMID:23192026[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hughes RC, McFeeters H, Coates L, McFeeters RL. Recombinant production, crystallization and X-ray crystallographic structure determination of the peptidyl-tRNA hydrolase of Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1472-6., doi: 10.1107/S1744309112045770. Epub 2012 Nov 28. PMID:23192026 doi:http://dx.doi.org/10.1107/S1744309112045770
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