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New page: left|200px<br /><applet load="2e7y" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e7y, resolution 1.97Å" /> '''High resolution stru...
 
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[[Image:2e7y.jpg|left|200px]]<br /><applet load="2e7y" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2e7y, resolution 1.97&Aring;" />
'''High resolution structure of T. maritima tRNase Z'''<br />


==Overview==
==High resolution structure of T. maritima tRNase Z==
tRNA 3'-processing endoribonuclease (tRNase Z) is one of the enzymes, involved in the 3'-end processing of precursor tRNAs and is a member of, the metallo-beta-lactamase superfamily. tRNase Z crystal structures have, revealed that the enzyme forms a dimer and has a characteristic domain, named a flexible arm or an exosite, which protrudes from the, metallo-beta-lactamase core and is involved in tRNA binding. The refined, structure of Thermotoga maritima tRNase Z has been determined at 1.97 A, resolution, revealing the structure of the flexible arm and the zinc-bound, active site. The structure of the flexible arm of T. maritima tRNase Z is, distinct from those of the Bacillus subtilis and Escherichia coli tRNase, Zs. A comparison of the three tRNase Z structures revealed differences in, the dimer orientation, which may be related to the unique cleavage-site, specificity of T. maritima tRNase Z.
<StructureSection load='2e7y' size='340' side='right'caption='[[2e7y]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2e7y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E7Y FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2e7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e7y OCA], [https://pdbe.org/2e7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e7y RCSB], [https://www.ebi.ac.uk/pdbsum/2e7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e7y ProSAT], [https://www.topsan.org/Proteins/RSGI/2e7y TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9WZW8_THEMA Q9WZW8_THEMA]
== 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/e7/2e7y_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=2e7y ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
tRNA 3'-processing endoribonuclease (tRNase Z) is one of the enzymes involved in the 3'-end processing of precursor tRNAs and is a member of the metallo-beta-lactamase superfamily. tRNase Z crystal structures have revealed that the enzyme forms a dimer and has a characteristic domain, named a flexible arm or an exosite, which protrudes from the metallo-beta-lactamase core and is involved in tRNA binding. The refined structure of Thermotoga maritima tRNase Z has been determined at 1.97 A resolution, revealing the structure of the flexible arm and the zinc-bound active site. The structure of the flexible arm of T. maritima tRNase Z is distinct from those of the Bacillus subtilis and Escherichia coli tRNase Zs. A comparison of the three tRNase Z structures revealed differences in the dimer orientation, which may be related to the unique cleavage-site specificity of T. maritima tRNase Z.


==About this Structure==
The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes.,Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):637-41. Epub 2007 Jul 21. PMID:17671357<ref>PMID:17671357</ref>
2E7Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PGO:'>PGO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_Z Ribonuclease Z], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.11 3.1.26.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Y OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes., Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M, Yokoyama S, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):637-41. Epub 2007 Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17671357 17671357]
</div>
[[Category: Ribonuclease Z]]
<div class="pdbe-citations 2e7y" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
 
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Ishii, R.]]
[[Category: Ishii R]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S.]]
[[Category: PGO]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: hydrolase]]
[[Category: metallo-beta-lactamse]]
[[Category: national project on protein structural and functional analyses]]
[[Category: nppsfa]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rnase]]
[[Category: rsgi]]
[[Category: structural genomics]]
[[Category: trna maturation]]
 
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Latest revision as of 08:36, 25 October 2023

High resolution structure of T. maritima tRNase Z

2e7y, resolution 1.97Å

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