2pid

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{{STRUCTURE_2pid| PDB=2pid | SCENE= }}
 
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===Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog===
 
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{{ABSTRACT_PUBMED_17997975}}
 
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==Disease==
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==Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog==
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[[http://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:[http://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>
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<StructureSection load='2pid' size='340' side='right'caption='[[2pid]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<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>
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[[http://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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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==About this Structure==
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<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>
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[[2pid]] is a 2 chain structure with sequence from [http://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].
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</table>
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== Disease ==
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[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>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pi/2pid_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017997975</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Tyrosine--tRNA ligase]]
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[[Category: Large Structures]]
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[[Category: Bonnefond, L.]]
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[[Category: Bonnefond L]]
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[[Category: Florentz, C.]]
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[[Category: Florentz C]]
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[[Category: Frugier, M.]]
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[[Category: Frugier M]]
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[[Category: Giege, R.]]
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[[Category: Giege R]]
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[[Category: Lorber, B.]]
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[[Category: Lorber B]]
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[[Category: Rudinger-Thirion, J.]]
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[[Category: Rudinger-Thirion J]]
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[[Category: Sauter, C.]]
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[[Category: Sauter C]]
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[[Category: Touze, E.]]
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[[Category: Touze E]]
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[[Category: Aminoacyl-trna synthetase]]
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[[Category: Atp-binding]]
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[[Category: Ligase]]
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[[Category: Mitochondrion]]
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[[Category: Nucleotide-binding]]
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[[Category: Protein biosynthesis]]
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[[Category: Protein-substrate complex]]
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Current revision

Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog

PDB ID 2pid

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