3hxu
From Proteopedia
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- | [[Image:3hxu.png|left|200px]] | ||
- | < | + | ==Crystal Structure of catalytic fragment of E. coli AlaRS in complex with AlaSA== |
- | + | <StructureSection load='3hxu' size='340' side='right'caption='[[3hxu]], [[Resolution|resolution]] 2.10Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3hxu]] 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=3HXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HXU FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |
- | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A5A:5-O-(N-(L-ALANYL)-SULFAMOYL)ADENOSINE'>A5A</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></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=3hxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hxu OCA], [https://pdbe.org/3hxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hxu RCSB], [https://www.ebi.ac.uk/pdbsum/3hxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hxu 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/3hxu_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=3hxu ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | [[Category: Escherichia coli K-12]] | |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Guo M]] | |
- | + | [[Category: Schimmel P]] | |
- | [[ | + | [[Category: Yang X-L]] |
- | + | ||
- | == | + | |
- | < | + | |
- | [[Category: | + | |
- | [[Category: | + | |
- | [[Category: Guo | + | |
- | [[Category: Schimmel | + | |
- | [[Category: Yang | + |
Current revision
Crystal Structure of catalytic fragment of E. coli AlaRS in complex with AlaSA
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