View source for 6iga


==Crystal structure of argininosuccinate lyase from Mycobacterium tuberculosis==
<StructureSection load='6iga' size='340' side='right'caption='[[6iga]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iga]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IGA 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]] 2.776&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6iga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iga OCA], [https://pdbe.org/6iga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iga RCSB], [https://www.ebi.ac.uk/pdbsum/6iga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iga ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARLY_MYCTU ARLY_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Argininosuccinate lyase (ASL) participates in arginine synthesis through catalysing a reversible reaction in which argininosuccinate (AS) converts into arginine and fumarate. ASL from Mycobacterium tuberculosis is essential for its growth. In this work, the crystal structure of the apo form of MtbASL was determined and reveals a tetrameric structure that is essential for its activity since the active sites are formed by residues from three different monomers. Subsequently, we determined the crystal structure of MtbASL-sulfate complex, and the ligand mimics the negatively charged intermediate. The complex structure and mutagenesis studies indicate that residues S282 and H161 might act as a catalytic dyad. A major conformational change in the MtbASL-SO4 complex structure could be observed upon sulfate binding, and this movement facilitates the interaction between substrate and the residues involved in catalysis. A different conformational change in the C-terminal domain could be observed in the MtbASL-SO4 complex compared with that in other homologues. This difference may be responsible for the lower activity of MtbASL, which is related to the slow growth rate of M. tuberculosis. The C-terminal domain is a potential allosteric site upon inhibitor binding. The various conformational changes and the diversity of the sequence of the potential allosteric site across the homologues might provide clues for designing selective inhibitors against M. tuberculosis.

Crystal structure and biochemical study on argininosuccinate lyase from Mycobacterium tuberculosis.,Chen X, Chen J, Zhang W, Wang H, Liu X, Zhou W, Yang H, Rao Z Biochem Biophys Res Commun. 2019 Feb 26;510(1):116-121. doi:, 10.1016/j.bbrc.2019.01.061. Epub 2019 Jan 18. PMID:30665717<ref>PMID:30665717</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iga" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Chen XB]]
[[Category: Liu X]]