7wwx: Difference between revisions

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New page: '''Unreleased structure''' The entry 7wwx is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 7wwx is ON HOLD
==Crystal structure of Herbaspirillum huttiense L-arabinose 1-dehydrogenase (NAD bound form)==
<StructureSection load='7wwx' size='340' side='right'caption='[[7wwx]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wwx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Herbaspirillum_huttiense_subsp._putei_IAM_15032 Herbaspirillum huttiense subsp. putei IAM 15032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WWX 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]] 1.36&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7wwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wwx OCA], [https://pdbe.org/7wwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wwx RCSB], [https://www.ebi.ac.uk/pdbsum/7wwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wwx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
l-Arabinose 1-dehydrogenase (AraDH) catalyzes the NAD(P)(+)-dependent oxidation of l-arabinose to L-arabinono-1,4-lactone in the non-phosphorylative l-arabinose pathway, and is classified into glucose-fructose oxidoreductase and short-chain dehydrogenase/reductase (SDR). We herein report the crystal structure of a SDR-type AraDH (from Herbaspirillum huttiense) for the first time. The interactions between Asp49 and the 2'- and 3'-hydroxyl groups of NAD(+) were consistent with strict specificity for NAD(+). In a binding model for the substrate, Ser155 and Tyr168, highly conserved in the SDR superfamily, interacted with the C1 and/or C2 hydroxyl(s) of l-arabinose, whereas interactions between Asp107, Arg109, and Gln206 and the C2 and/or C3 hydroxyl(s) were unique to AraDH. Trp200 significantly contributed to the selectivities of the C4 hydroxyl and C6 methyl of substrates.


Authors:  
Crystal structure of L-arabinose 1-dehydrogenase as a short-chain reductase/dehydrogenase protein.,Watanabe S, Yoshiwara K, Matsubara R, Watanabe Y Biochem Biophys Res Commun. 2022 Mar 8;604:14-21. doi:, 10.1016/j.bbrc.2022.03.028. PMID:35279441<ref>PMID:35279441</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7wwx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Herbaspirillum huttiense subsp. putei IAM 15032]]
[[Category: Large Structures]]
[[Category: Matsubara R]]
[[Category: Watanabe S]]
[[Category: Watanabe Y]]
[[Category: Yoshiwara K]]