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4lns

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<StructureSection load='4lns' size='340' side='right'caption='[[4lns]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='4lns' size='340' side='right'caption='[[4lns]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lns]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LNS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4lns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei_TREU927 Trypanosoma brucei brucei TREU927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LNS FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[11as|11as]]</td></tr>
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</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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lns OCA], [https://pdbe.org/4lns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lns RCSB], [https://www.ebi.ac.uk/pdbsum/4lns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lns ProSAT]</span></td></tr>
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<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=4lns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lns OCA], [http://pdbe.org/4lns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lns RCSB], [http://www.ebi.ac.uk/pdbsum/4lns PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lns ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q57WT9_TRYB2 Q57WT9_TRYB2]
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Asparagine is formed by two structurally distinct asparagine synthetases in prokaryotes. One is the ammonia-utilizing asparagine synthetase A (AsnA), and the other is asparagine synthetase B (AsnB) that uses glutamine or ammonia as a nitrogen source. In a previous investigation using sequence-based analysis, we had shown that Leishmania spp. possess asparagine-tRNA synthetase paralog asparagine synthetase A (LdASNA) that is ammonia-dependent. Here, we report the cloning, expression, and kinetic analysis of ASNA from Leishmania donovani. Interestingly, LdASNA was both ammonia- and glutamine-dependent. To study the physiological role of ASNA in Leishmania, gene deletion mutations were attempted via targeted gene replacement. Gene deletion of LdASNA showed a growth delay in mutants. However, chromosomal null mutants of LdASNA could not be obtained as the double transfectant mutants showed aneuploidy. These data suggest that LdASNA is essential for survival of the Leishmania parasite. LdASNA enzyme was recalcitrant toward crystallization so we instead crystallized and solved the atomic structure of its close homolog from Trypanosoma brucei (TbASNA) at 2.2 A. A very significant conservation in active site residues is observed between TbASNA and Escherichia coli AsnA. It is evident that the absence of an LdASNA homolog from humans and its essentiality for the parasites make LdASNA a novel drug target.
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Identification and functional characterization of a novel bacterial type asparagine synthetase A: a tRNA synthetase paralog from Leishmania donovani.,Manhas R, Tripathi P, Khan S, Sethu Lakshmi B, Lal SK, Gowri VS, Sharma A, Madhubala R J Biol Chem. 2014 Apr 25;289(17):12096-108. doi: 10.1074/jbc.M114.554642. Epub, 2014 Mar 7. PMID:24610810<ref>PMID:24610810</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4lns" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspartate--ammonia ligase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Khan, S]]
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[[Category: Trypanosoma brucei brucei TREU927]]
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[[Category: Madhubala, R]]
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[[Category: Khan S]]
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[[Category: Sharma, A]]
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[[Category: Madhubala R]]
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[[Category: Asparagine synthetase some]]
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[[Category: Sharma A]]
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[[Category: Ligase]]
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Current revision

Crystal structure of Asparagine synthetase A (AsnA) from Trypanosoma brucei

PDB ID 4lns

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