View source for 4ijc


==Crystal structure of arabinose dehydrogenase Ara1 from Saccharomyces cerevisiae==
<StructureSection load='4ijc' size='340' side='right'caption='[[4ijc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ijc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IJC 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4ijc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijc OCA], [https://pdbe.org/4ijc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ijc RCSB], [https://www.ebi.ac.uk/pdbsum/4ijc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ijc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARA1_YEAST ARA1_YEAST] Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose and L-galactose in the presence of NADP(+).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The primary role of yeast Ara1, previously mis-annotated as a D-arabinose dehydrogenase, is to catalyze the reduction of a variety of toxic alpha,beta-dicarbonyl compounds using NADPH as a cofactor at physiological pH levels. Here, crystal structures of Ara1 in apo and NADPH-complexed forms are presented at 2.10 and 2.00 A resolution, respectively. Ara1 exists as a homodimer, each subunit of which adopts an (alpha/beta)8-barrel structure and has a highly conserved cofactor-binding pocket. Structural comparison revealed that induced fit upon NADPH binding yielded an intact active-site pocket that recognizes the substrate. Moreover, the crystal structures combined with computational simulation defined an open substrate-binding site to accommodate various substrates that possess a dicarbonyl group.

Structures of Saccharomyces cerevisiaeD-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition.,Hu XQ, Guo PC, Ma JD, Li WF Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1190-5. doi:, 10.1107/S1744309113026857. Epub 2013 Oct 26. PMID:24192347<ref>PMID:24192347</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ijc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Guo PC]]
[[Category: Hu XQ]]
[[Category: Li WF]]
[[Category: Zhou CZ]]