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[[Image:12as.gif|left|200px]]
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{{STRUCTURE_12as|  PDB=12as  |  SCENE=  }}
'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP'''


==ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP==
<StructureSection load='12as' size='340' side='right'caption='[[12as]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[12as]] 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=12AS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=12AS 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <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=12as FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=12as OCA], [https://pdbe.org/12as PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=12as RCSB], [https://www.ebi.ac.uk/pdbsum/12as PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=12as 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/2a/12as_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=12as ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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:9437423<ref>PMID:9437423</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
12AS is a [[Single protein]] structure of 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=12AS OCA].
</div>
<div class="pdbe-citations 12as" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/9437423 9437423]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
[[Category: Aspartate--ammonia ligase]]
== References ==
[[Category: Escherichia coli]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Kato, H.]]
</StructureSection>
[[Category: Nakatsu, T.]]
[[Category: Escherichia coli K-12]]
[[Category: Oda, J.]]
[[Category: Large Structures]]
[[Category: Asparagine synthetase]]
[[Category: Kato H]]
[[Category: Ligase]]
[[Category: Nakatsu T]]
[[Category: Nitrogen fixation]]
[[Category: Oda J]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:28:28 2008''
Retrieved from "https://proteopedia.org/12as"