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New page: left|200px<br /><applet load="11as" size="450" color="white" frame="true" align="right" spinBox="true" caption="11as, resolution 2.5Å" /> '''ASPARAGINE SYNTHETASE...
 
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[[Image:11as.jpg|left|200px]]<br /><applet load="11as" size="450" color="white" frame="true" align="right" spinBox="true"
caption="11as, resolution 2.5&Aring;" />
'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE'''<br />


==Overview==
==ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE==
The crystal structure of E. coli asparagine synthetase has been determined, by X-ray diffraction analysis at 2.5 A resolution. The overall structure, of the enzyme is remarkably similar to that of the catalytic domain of, yeast aspartyl-tRNA synthetase despite low sequence similarity. These, enzymes have a common reaction mechanism that implies the formation of an, aminoacyl-adenylate intermediate. The active site architecture and most of, the catalytic residues are also conserved in both enzymes. These proteins, have probably evolved from a common ancestor even though their sequence, similarities are small. The functional and structural similarities of both, enzymes suggest that new enzymatic activities would generally follow the, recruitment of a protein catalyzing a similar chemical reaction.
<StructureSection load='11as' size='340' side='right'caption='[[11as]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[11as]] is a 2 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=11AS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=11AS 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASN:ASPARAGINE'>ASN</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=11as FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=11as OCA], [https://pdbe.org/11as PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=11as RCSB], [https://www.ebi.ac.uk/pdbsum/11as PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=11as ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASNA_ECOLI ASNA_ECOLI] May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn (Probable).<ref>PMID:17962566</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/1a/11as_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=11as ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
11AS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ASN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate--ammonia_ligase Aspartate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.1 6.3.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=11AS OCA].
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase., Nakatsu T, Kato H, Oda J, Nat Struct Biol. 1998 Jan;5(1):15-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9437423 9437423]
__TOC__
[[Category: Aspartate--ammonia ligase]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli K-12]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kato, H.]]
[[Category: Kato H]]
[[Category: Nakatsu, T.]]
[[Category: Nakatsu T]]
[[Category: Oda, J.]]
[[Category: Oda J]]
[[Category: ASN]]
[[Category: asparagine synthetase]]
[[Category: ligase]]
[[Category: nitrogen fixation]]
 
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Retrieved from "https://proteopedia.org/11as"