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[[Image:3hxx.png|left|200px]]


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==Crystal Structure of catalytic fragment of E. coli AlaRS in complex with AMPPCP==
The line below this paragraph, containing "STRUCTURE_3hxx", creates the "Structure Box" on the page.
<StructureSection load='3hxx' size='340' side='right'caption='[[3hxx]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3hxx]] is a 1 chain structure with sequence from [https://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=3HXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HXX FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11&#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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_3hxx| PDB=3hxx |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hxx OCA], [https://pdbe.org/3hxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hxx RCSB], [https://www.ebi.ac.uk/pdbsum/3hxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hxx ProSAT]</span></td></tr>
</table>
== Function ==
[https://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>  
== 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/hx/3hxx_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=3hxx ConSurf].
<div style="clear:both"></div>


===Crystal Structure of catalytic fragment of E. coli AlaRS in complex with AMPPCP===
==See Also==
 
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
== References ==
<!--
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[[Category: Escherichia coli K-12]]
{{ABSTRACT_PUBMED_20010690}}
[[Category: Large Structures]]
 
[[Category: Guo M]]
==About this Structure==
[[Category: Schimmel P]]
[[3hxx]] is a 1 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=3HXX OCA].
[[Category: Yang X-L]]
 
==Reference==
<ref group="xtra">PMID:20010690</ref><references group="xtra"/>
[[Category: Alanine--tRNA ligase]]
[[Category: Escherichia coli]]
[[Category: Guo, M.]]
[[Category: Schimmel, P.]]
[[Category: Yang, X L.]]

Latest revision as of 13:02, 21 February 2024

Crystal Structure of catalytic fragment of E. coli AlaRS in complex with AMPPCPCrystal Structure of catalytic fragment of E. coli AlaRS in complex with AMPPCP

Structural highlights

3hxx is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.11Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  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

3hxx, resolution 2.11Å

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