2pid

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[[Image:2pid.png|left|200px]]
 
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{{STRUCTURE_2pid| PDB=2pid | SCENE= }}
{{STRUCTURE_2pid| PDB=2pid | SCENE= }}
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===Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog===
===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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{{ABSTRACT_PUBMED_17997975}}
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==Disease==
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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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==Function==
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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>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:017997975</ref><references group="xtra"/>
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<ref group="xtra">PMID:017997975</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Tyrosine--tRNA ligase]]
[[Category: Tyrosine--tRNA ligase]]

Revision as of 02:24, 25 March 2013

Template:STRUCTURE 2pid

Contents

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

Template:ABSTRACT PUBMED 17997975

Disease

[SYYM_HUMAN] Defects in YARS2 are the cause of myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2) [MIM: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.[1][2]

Function

[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).[3]

About this Structure

2pid is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Bonnefond L, Frugier M, Touze E, Lorber B, Florentz C, Giege R, Sauter C, Rudinger-Thirion J. Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features. Structure. 2007 Nov;15(11):1505-16. PMID:17997975 doi:10.1016/j.str.2007.09.018
  1. ↑ Riley LG, Cooper S, Hickey P, Rudinger-Thirion J, McKenzie M, Compton A, Lim SC, Thorburn D, Ryan MT, Giege R, Bahlo M, Christodoulou J. Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome. Am J Hum Genet. 2010 Jul 9;87(1):52-9. doi: 10.1016/j.ajhg.2010.06.001. PMID:20598274 doi:10.1016/j.ajhg.2010.06.001
  2. ↑ Sasarman F, Nishimura T, Thiffault I, Shoubridge EA. A novel mutation in YARS2 causes myopathy with lactic acidosis and sideroblastic anemia. Hum Mutat. 2012 Aug;33(8):1201-6. doi: 10.1002/humu.22098. Epub 2012 May 7. PMID:22504945 doi:10.1002/humu.22098
  3. ↑ Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M. Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. PMID:15779907 doi:10.1021/bi047527z

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