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| | <StructureSection load='4qt4' size='340' side='right'caption='[[4qt4]], [[Resolution|resolution]] 2.19Å' scene=''> | | <StructureSection load='4qt4' size='340' side='right'caption='[[4qt4]], [[Resolution|resolution]] 2.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qt4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpz Strpz]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4q55 4q55]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QT4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qt4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_NZ131 Streptococcus pyogenes NZ131]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4q55 4q55]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QT4 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jc4|4jc4]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pth, Spy49_0005 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471876 STRPZ])</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=4qt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qt4 OCA], [https://pdbe.org/4qt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qt4 RCSB], [https://www.ebi.ac.uk/pdbsum/4qt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qt4 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=4qt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qt4 OCA], [http://pdbe.org/4qt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4qt4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qt4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PTH_STRPZ PTH_STRPZ]] 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_STRPZ PTH_STRPZ] 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aminoacyl-tRNA hydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strpz]] | + | [[Category: Streptococcus pyogenes NZ131]] |
| - | [[Category: Bhushan, A]] | + | [[Category: Bhushan A]] |
| - | [[Category: Gautam, L]] | + | [[Category: Gautam L]] |
| - | [[Category: Kaur, P]] | + | [[Category: Kaur P]] |
| - | [[Category: Sharma, S]] | + | [[Category: Sharma S]] |
| - | [[Category: Singh, A]] | + | [[Category: Singh A]] |
| - | [[Category: Singh, T P]] | + | [[Category: Singh TP]] |
| - | [[Category: Sinha, M]] | + | [[Category: Sinha M]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Peptidyl-trna]]
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| - | [[Category: Pth]]
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| Structural highlights
Function
PTH_STRPZ The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).
Publication Abstract from PubMed
Peptidyl-tRNA hydrolase (Pth) catalyses the release of tRNA and peptide components from peptidyl-tRNA molecules. Pth from a Gram-positive bacterium Streptococcus pyogenes (SpPth) was cloned, expressed, purified and crystallised. Three-dimensional structure of SpPth was determined by X-ray crystallography at 2.19 A resolution. Structure determination showed that the asymmetric unit of the unit cell contained two crystallographically independent molecules, designated A and B. The superimposition of C(alpha) traces of molecules A and B showed an r.m.s. shift of 0.4 A, indicating that the structures of two crystallographically independent molecules were identical. The polypeptide chain of SpPth adopted an overall alpha/beta conformation. The substrate-binding cleft in SpPth is formed with three loops: the gate loop, Ile91-Leu102; the base loop, Gly108-Gly115; and the lid loop, Gly136-Gly150. Unlike in the structures of Pth from Gram-negative bacteria, the entry to the cleft in the structure of SpPth appeared to be virtually closed. However, the conformations of the active site residues were found to be similar.
Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 A resolution shows the closed structure of the substrate-binding cleft.,Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP FEBS Open Bio. 2014 Oct 22;4:915-22. doi: 10.1016/j.fob.2014.10.010. eCollection , 2014. PMID:25389518[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP. Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 A resolution shows the closed structure of the substrate-binding cleft. FEBS Open Bio. 2014 Oct 22;4:915-22. doi: 10.1016/j.fob.2014.10.010. eCollection , 2014. PMID:25389518 doi:http://dx.doi.org/10.1016/j.fob.2014.10.010
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