3o0a: Difference between revisions

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<StructureSection load='3o0a' size='340' side='right'caption='[[3o0a]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='3o0a' size='340' side='right'caption='[[3o0a]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o0a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O0A FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o0a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O0A FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuS, aq_351 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Leucine--tRNA_ligase Leucine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.4 6.1.1.4] </span></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=3o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0a OCA], [https://pdbe.org/3o0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o0a RCSB], [https://www.ebi.ac.uk/pdbsum/3o0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0a ProSAT]</span></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=3o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0a OCA], [https://pdbe.org/3o0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o0a RCSB], [https://www.ebi.ac.uk/pdbsum/3o0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0a ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/SYLA_AQUAE SYLA_AQUAE]
The editing or hydrolytic CP1 domain of leucyl-tRNA synthetase (LeuRS) hydrolyses several misactivated amino acids. The CP1 domain of Aquifex aeolicus LeuRS was expressed, purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.8, b = 98.4, c = 116.7 A. Crystals diffract to beyond 1.8 A resolution and contain two monomers in the asymmetric unit. Two CP1 mutants in which a conserved threonine residue essential for the fidelity of the hydrolytic pathway is mutated to alanine or glutamic acid have also been expressed and crystallized. Crystals of the two CP1 mutants are isomorphs of the wild type and diffract to beyond 1.9 A resolution. All structures were solved by molecular-replacement techniques.
 
Crystallization and preliminary X-ray crystallographic study of the wild type and two mutants of the CP1 hydrolytic domain from Aquifex aeolicus leucyl-tRNA synthetase.,Cura V, Olieric N, Guichard A, Wang ED, Moras D, Eriani G, Cavarelli J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Oct 1;61(Pt, 10):899-901. Epub 2005 Sep 13. PMID:16511190<ref>PMID:16511190</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3o0a" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aquifex aeolicus huber and stetter 2001]]
[[Category: Aquifex aeolicus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Leucine--tRNA ligase]]
[[Category: Cavarelli J]]
[[Category: Cavarelli, J]]
[[Category: Cura V]]
[[Category: Cura, V]]
[[Category: Eriani G]]
[[Category: Eriani, G]]
[[Category: Moras D]]
[[Category: Moras, D]]
[[Category: Olieric N]]
[[Category: Olieric, N]]
[[Category: Wang E-D]]
[[Category: Wang, E D]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Aquifex aeolicus]]
[[Category: Atp-binding]]
[[Category: Cp1 hydrolytic domain]]
[[Category: Leucyl-trna synthetase]]
[[Category: Ligase]]
[[Category: Nucleotide-binding]]
[[Category: Protein biosynthesis]]

Revision as of 12:25, 6 September 2023

Crystal structure of the wild type CP1 hydrolitic domain from Aquifex Aeolicus leucyl-trnaCrystal structure of the wild type CP1 hydrolitic domain from Aquifex Aeolicus leucyl-trna

Structural highlights

3o0a is a 2 chain structure with sequence from Aquifex aeolicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.77Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYLA_AQUAE

See Also

3o0a, resolution 1.77Å

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