5ax8: Difference between revisions

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New page: '''Unreleased structure''' The entry 5ax8 is ON HOLD Authors: Jiang, X., Wang, J., Chang, H., Zhou, Y. Description: Recombinant expression, purification and preliminary crystallographi...
 
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'''Unreleased structure'''


The entry 5ax8 is ON HOLD
==Recombinant expression, purification and preliminary crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase==
<StructureSection load='5ax8' size='340' side='right'caption='[[5ax8]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ax8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AX8 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]] 2.989&#8491;</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=5ax8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ax8 OCA], [https://pdbe.org/5ax8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ax8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ax8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ax8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AATM_HUMAN AATM_HUMAN] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.<ref>PMID:9537447</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mitochondrial aspartate aminotransferase (mAspAT) was recognized as a moonlighting enzyme because it has not only aminotransferase activity but also a high-affinity long-chain fatty acids (LCFA) binding site. This enzyme plays a key role in amino acid metabolism, biosynthesis of kynurenic acid and transport of the LCFA. Therefore, it is important to study the structure-function relationships of human mAspAT protein. In this work, the mature form of human mAspAT was expressed to a high level in Escherichia coli periplasmic space using pET-22b vector, purified by a combination of immobilized metal-affinity chromatography and cation exchange chromatography. Optimal activity of the enzyme occurred at a temperature of 47.5 masculineC and a pH of 8.5. Crystals of human mAspAT were grown using the hanging-drop vapour diffusion method at 277K with 0.1 M HEPES pH 6.8 and 25%(v/v) Jeffamine((R)) ED-2001 pH 6.8. The crystals diffracted to 2.99 A and belonged to the space group P1 with the unit-cell parameters a =56.7, b = 76.1, c = 94.2 A, alpha =78.0, beta =85.6, gamma = 78.4 masculine. Elucidation of mAspAT structure can provide a molecular basis towards understanding catalysis mechanism and substrate binding site of enzyme.


Authors: Jiang, X., Wang, J., Chang, H., Zhou, Y.
Recombinant expression, purification and crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase.,Jiang X, Wang J, Chang H, Zhou Y Biosci Trends. 2016 Mar 10;10(1):79-84. doi: 10.5582/bst.2015.01150. Epub 2016, Feb 22. PMID:26902786<ref>PMID:26902786</ref>


Description: Recombinant expression, purification and preliminary crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Wang, J]]
<div class="pdbe-citations 5ax8" style="background-color:#fffaf0;"></div>
[[Category: Jiang, X]]
 
[[Category: Chang, H]]
==See Also==
[[Category: Zhou, Y]]
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chang H]]
[[Category: Jiang X]]
[[Category: Wang J]]
[[Category: Zhou Y]]
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