2pid: Difference between revisions
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New page: left|200px<br /> <applet load="2pid" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pid, resolution 2.20Å" /> '''Crystal structure o... |
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== | ==Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog== | ||
<StructureSection load='2pid' size='340' side='right'caption='[[2pid]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2pid]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PID 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YSA:5-O-[N-(L-TYROSYL)SULFAMOYL]ADENOSINE'>YSA</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=2pid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pid OCA], [https://pdbe.org/2pid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pid RCSB], [https://www.ebi.ac.uk/pdbsum/2pid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pid ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/SYYM_HUMAN SYYM_HUMAN] Defects in YARS2 are the cause of myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2) [MIM:[https://omim.org/entry/613561 613561]. MLASA2 is a rare oxidative phosphorylation disorder specific to skeletal muscle and bone marrow. Affected individuals manifest sideroblastic anemia, progressive lethargy, muscle weakness, and exercise intolerance associated with persistent lactic acidemia.<ref>PMID:20598274</ref> <ref>PMID:22504945</ref> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SYYM_HUMAN SYYM_HUMAN] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity).<ref>PMID:15779907</ref> | |||
== 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/pi/2pid_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=2pid ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bonnefond L]] | |||
[[Category: Bonnefond | [[Category: Florentz C]] | ||
[[Category: Florentz | [[Category: Frugier M]] | ||
[[Category: Frugier | [[Category: Giege R]] | ||
[[Category: Giege | [[Category: Lorber B]] | ||
[[Category: Lorber | [[Category: Rudinger-Thirion J]] | ||
[[Category: Rudinger-Thirion | [[Category: Sauter C]] | ||
[[Category: Sauter | [[Category: Touze E]] | ||
[[Category: Touze | |||