2jrc
From Proteopedia
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| - | {{Large structure}} | ||
| - | {{STRUCTURE_2jrc| PDB=2jrc | SCENE= }} | ||
| - | ===Solution structure of Peptidyl-tRNA Hydrolase from Mycobacterium tuberculosis H37Rv.=== | ||
| - | {{ABSTRACT_PUBMED_18342886}} | ||
| - | == | + | ==Solution structure of Peptidyl-tRNA Hydrolase from Mycobacterium tuberculosis H37Rv.== |
| - | [[2jrc]] is a 1 chain structure with sequence from [ | + | <StructureSection load='2jrc' size='340' side='right'caption='[[2jrc]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2jrc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JRC FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jrc OCA], [https://pdbe.org/2jrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jrc RCSB], [https://www.ebi.ac.uk/pdbsum/2jrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jrc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PTH_MYCTU PTH_MYCTU] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jr/2jrc_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jrc ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Eubacterial peptidyl-tRNA hydrolase is an essential enzyme that hydrolyzes peptidyl-tRNAs that are released into the cytoplasm because of premature termination of translation, expression of minigenes, and action of lincosamide and macrolide antibiotics. This averts the arrest of protein synthesis caused by depletion of free tRNA. Recently, we demonstrated that Mycobacterium tuberculosis peptidyl-tRNA hydrolase (MtPth) is present in the cytosol of mycobacterium and is capable of hydrolyzing peptidyl-tRNA. Here, we present the solution structure of MtPth, which is the first solution structure for this family of proteins. MtPth typically consists of seven-stranded mixed beta-sheet surrounded by six alpha-helices. The backbone dynamics for this enzyme were probed by measuring (15)N relaxation parameters and these were analyzed with model-free formalism and reduced spectral density mapping analysis. Overall, the protein molecule has tau(m) of 9.67+/-0.02 ns. The (15)N relaxation data analysis reveals that while majority of the protein backbone is rigid to motions, a short segment consisting of enzymatically critical residue H22, the loop-helix cover over the active site crevice, and the C-terminal helical hairpin exhibit motions on the milli-to microsecond timescale, all of which are linked to interaction with the substrate peptidyl-tRNA. | ||
| - | + | Solution structure and dynamics of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis H37Rv.,Pulavarti SV, Jain A, Pathak PP, Mahmood A, Arora A J Mol Biol. 2008 Apr 18;378(1):165-77. Epub 2008 Feb 21. PMID:18342886<ref>PMID:18342886</ref> | |
| - | <ref | + | |
| - | [[ | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2jrc" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | [[Category: | + | ==See Also== |
| - | [[Category: | + | *[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]] |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
| + | [[Category: Arora A]] | ||
| + | [[Category: Jain A]] | ||
| + | [[Category: Pathak PP]] | ||
| + | [[Category: Pulavarti SVSRK]] | ||
Current revision
Solution structure of Peptidyl-tRNA Hydrolase from Mycobacterium tuberculosis H37Rv.
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