3rl6: Difference between revisions
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==Crystal structure of the archaeal asparagine synthetase A complexed with L-Asparagine and Adenosine monophosphate== | ==Crystal structure of the archaeal asparagine synthetase A complexed with L-Asparagine and Adenosine monophosphate== | ||
<StructureSection load='3rl6' size='340' side='right' caption='[[3rl6]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3rl6' size='340' side='right' caption='[[3rl6]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rl6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3rl6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrab Pyrab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RL6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asnS-like, PYRAB02460, PAB2356 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asnS-like, PYRAB02460, PAB2356 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272844 PYRAB])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rl6 RCSB], [http://www.ebi.ac.uk/pdbsum/3rl6 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl6 OCA], [http://pdbe.org/3rl6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rl6 RCSB], [http://www.ebi.ac.uk/pdbsum/3rl6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rl6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3rl6" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Pyrab]] | ||
[[Category: Blaise, M]] | [[Category: Blaise, M]] | ||
[[Category: Charron, C]] | [[Category: Charron, C]] | ||
Revision as of 20:35, 11 August 2016
Crystal structure of the archaeal asparagine synthetase A complexed with L-Asparagine and Adenosine monophosphateCrystal structure of the archaeal asparagine synthetase A complexed with L-Asparagine and Adenosine monophosphate
Structural highlights
Publication Abstract from PubMedAsparagine synthetase A (AsnA) catalyzes asparagine synthesis using aspartate, ATP, and ammonia as substrates. Asparagine is formed in two steps: the beta-carboxylate group of aspartate is first activated by ATP to form an aminoacyl-AMP before its amidation by a nucleophilic attack with an ammonium ion. Interestingly, this mechanism of amino acid activation resembles that used by aminoacyl-tRNA synthetases, which first activate the alpha-carboxylate group of the amino acid to form also an aminoacyl-AMP before they transfer the activated amino acid onto the cognate tRNA. In a previous investigation, we have shown that the open reading frame of Pyrococcus abyssi annotated as asparaginyl-tRNA synthetase (AsnRS) 2 is, in fact, an archaeal asparagine synthetase A (AS-AR) that evolved from an ancestral aspartyl-tRNA synthetase (AspRS). We present here the crystal structure of this AS-AR. The fold of this protein is similar to that of bacterial AsnA and resembles the catalytic cores of AspRS and AsnRS. The high-resolution structures of AS-AR associated with its substrates and end-products help to understand the reaction mechanism of asparagine formation and release. A comparison of the catalytic core of AS-AR with those of archaeal AspRS and AsnRS and with that of bacterial AsnA reveals a strong conservation. This study uncovers how the active site of the ancestral AspRS rearranged throughout evolution to transform an enzyme activating the alpha-carboxylate group into an enzyme that is able to activate the beta-carboxylate group of aspartate, which can react with ammonia instead of tRNA. Crystal Structure of the Archaeal Asparagine Synthetase: Interrelation with Aspartyl-tRNA and Asparaginyl-tRNA Synthetases.,Blaise M, Frechin M, Olieric V, Charron C, Sauter C, Lorber B, Roy H, Kern D J Mol Biol. 2011 Sep 23;412(3):437-52. Epub 2011 Jul 28. PMID:21820443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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