View source for 5oyn


==Crystal structure of D-xylonate dehydratase in holo-form==
<StructureSection load='5oyn' size='340' side='right'caption='[[5oyn]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5oyn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_CB15 Caulobacter vibrioides CB15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OYN 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5oyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oyn OCA], [https://pdbe.org/5oyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oyn RCSB], [https://www.ebi.ac.uk/pdbsum/5oyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oyn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYLD_CAUVC XYLD_CAUVC] Catalyzes the dehydration of D-xylonate to 2-dehydro-3-deoxy-D-arabinonate during D-xylose degradation. Can also dehydrate D-gluconate, with similar catalytic efficiency. Has weak activity with D-galactonate, D-fuconate and L-arabinonate.<ref>PMID:27102126</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Ilv/ED dehydratase protein family includes dihydroxy acid-, gluconate-, 6-phosphogluconate- and pentonate dehydratases. The members of this family are involved in various biosynthetic and carbohydrate metabolic pathways. Here, we describe the first crystal structure of D-xylonate dehydratase from Caulobacter crescentus (CcXyDHT) at 2.7 A resolution and compare it with other available enzyme structures from the IlvD/EDD protein family. The quaternary structure of CcXyDHT is a tetramer, and each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg(2+) ion. The active site is located at the monomer-monomer interface and contains residues from both the N-terminal recognition helix and the C-terminus of the dimeric counterpart. The active site also contains a conserved Ser490, which probably acts as a base in catalysis. Importantly, the cysteines that participate in the binding and formation of the [2Fe-2S] cluster are not all conserved within the Ilv/ED dehydratase family, which suggests that some members of the IlvD/EDD family may bind different types of [Fe-S] clusters.

The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family.,Rahman MM, Andberg M, Koivula A, Rouvinen J, Hakulinen N Sci Rep. 2018 Jan 16;8(1):865. doi: 10.1038/s41598-018-19192-6. PMID:29339766<ref>PMID:29339766</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5oyn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caulobacter vibrioides CB15]]
[[Category: Large Structures]]
[[Category: Hakulinen N]]
[[Category: Rahman MM]]
[[Category: Rouvinen J]]