View source for 4zhs


==Crystal Structure of Aspartate Semialdehyde Dehydrogenase from Trichophyton rubrum==
<StructureSection load='4zhs' size='340' side='right'caption='[[4zhs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zhs]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichophyton_rubrum_BMU01672 Trichophyton rubrum BMU01672]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZHS 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]] 2.603&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <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=4zhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zhs OCA], [https://pdbe.org/4zhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zhs RCSB], [https://www.ebi.ac.uk/pdbsum/4zhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zhs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A140UHG6_TRIRU A0A140UHG6_TRIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aspartate-beta-semialdehyde dehydrogenase (ASADH) catalyzes the second reaction in the aspartate pathway, a pathway required for the biosynthesis of one fifth of the essential amino acids in plants and microorganisms. Microarray analysis of a fungal pathogen T. rubrum responsible for most human dermatophytoses identified the upregulation of ASADH (trASADH) expression when the fungus is exposed to human skin, underscoring its potential as a drug target. Here we report the crystal structure of trASADH, revealing a tetrameric ASADH with a GAPDH-like fold. The tetramerization of trASADH was confirmed by sedimentation and SAXS experiments. Native PAGE demonstrated that this ASADH tetramerization is apparently universal in fungal species, unlike the functional dimer that is observed in all bacterial ASADHs. The helical subdomain in dimeric bacteria ASADH is replaced by the cover loop in archaeal/fungal ASADHs, presenting the determinant for this altered oligomerization. Mutations that disrupt the tetramerization of trASADH also abolish the catalytic activity, suggesting that the tetrameric state is required to produce the active fungal enzyme form. Our findings provide a basis to categorize ASADHs into dimeric and tetrameric enzymes, adopting a different orientation for NADP binding and offer a structural framework for designing drugs that can specifically target the fungal pathogens.

Structural Insights into the Tetrameric State of Aspartate-beta-semialdehyde Dehydrogenases from Fungal Species.,Li Q, Mu Z, Zhao R, Dahal G, Viola RE, Liu T, Jin Q, Cui S Sci Rep. 2016 Feb 12;6:21067. doi: 10.1038/srep21067. PMID:26869335<ref>PMID:26869335</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zhs" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
*[[Retinoid X receptor 3D structures|Retinoid X receptor 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Trichophyton rubrum BMU01672]]
[[Category: Cui S]]
[[Category: Li Q]]