3hy0

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[[Image:3hy0.png|left|200px]]
 
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{{STRUCTURE_3hy0| PDB=3hy0 | SCENE= }}
{{STRUCTURE_3hy0| PDB=3hy0 | SCENE= }}
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===Crystal Structure of catalytic fragment of E. coli AlaRS G237A in complex with GlySA===
===Crystal Structure of catalytic fragment of E. coli AlaRS G237A in complex with GlySA===
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{{ABSTRACT_PUBMED_20010690}}
{{ABSTRACT_PUBMED_20010690}}
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==Function==
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[[http://www.uniprot.org/uniprot/SYA_ECOLI SYA_ECOLI]] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller than alanine amino acid glycine as well as the sterically larger amino acid serine. These incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (glycine and serine) in the charging step.<ref>PMID:12554667</ref> <ref>PMID:18723508</ref> <ref>PMID:19661429</ref> Edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr).<ref>PMID:12554667</ref> <ref>PMID:18723508</ref> <ref>PMID:19661429</ref>
==About this Structure==
==About this Structure==
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[[3hy0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HY0 OCA].
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[[3hy0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HY0 OCA].
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==See Also==
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*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]
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==Reference==
==Reference==
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<ref group="xtra">PMID:020010690</ref><references group="xtra"/>
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<ref group="xtra">PMID:020010690</ref><references group="xtra"/><references/>
[[Category: Alanine--tRNA ligase]]
[[Category: Alanine--tRNA ligase]]
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli k-12]]
[[Category: Guo, M.]]
[[Category: Guo, M.]]
[[Category: Schimmel, P.]]
[[Category: Schimmel, P.]]

Revision as of 07:34, 20 June 2013

Template:STRUCTURE 3hy0

Contents

Crystal Structure of catalytic fragment of E. coli AlaRS G237A in complex with GlySA

Template:ABSTRACT PUBMED 20010690

Function

[SYA_ECOLI] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller than alanine amino acid glycine as well as the sterically larger amino acid serine. These incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (glycine and serine) in the charging step.[1] [2] [3] Edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr).[4] [5] [6]

About this Structure

3hy0 is a 2 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.

Reference

  • Guo M, Chong YE, Shapiro R, Beebe K, Yang XL, Schimmel P. Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. Nature. 2009 Dec 10;462(7274):808-12. PMID:20010690 doi:10.1038/nature08612
  1. ↑ Beebe K, Ribas De Pouplana L, Schimmel P. Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 2003 Feb 3;22(3):668-75. PMID:12554667 doi:10.1093/emboj/cdg065
  2. ↑ Chong YE, Yang XL, Schimmel P. Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. J Biol Chem. 2008 Oct 31;283(44):30073-8. doi: 10.1074/jbc.M805943200. Epub 2008 , Aug 22. PMID:18723508 doi:10.1074/jbc.M805943200
  3. ↑ Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. PMID:19661429 doi:325/5941/744
  4. ↑ Beebe K, Ribas De Pouplana L, Schimmel P. Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 2003 Feb 3;22(3):668-75. PMID:12554667 doi:10.1093/emboj/cdg065
  5. ↑ Chong YE, Yang XL, Schimmel P. Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. J Biol Chem. 2008 Oct 31;283(44):30073-8. doi: 10.1074/jbc.M805943200. Epub 2008 , Aug 22. PMID:18723508 doi:10.1074/jbc.M805943200
  6. ↑ Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. PMID:19661429 doi:325/5941/744

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