View source for 4hk5


==Crystal structure of Cordyceps militaris IDCase in apo form==
<StructureSection load='4hk5' size='340' side='right'caption='[[4hk5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hk5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cordyceps_militaris Cordyceps militaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HK5 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4hk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk5 OCA], [https://pdbe.org/4hk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hk5 RCSB], [https://www.ebi.ac.uk/pdbsum/4hk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hk5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G3J531_CORMM G3J531_CORMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DNA methylation and demethylation regulate many crucial biological processes in mammals and are linked to many diseases. Active DNA demethylation is believed to be catalyzed by TET proteins and a putative DNA decarboxylase that may share some similarities in sequence, structure and catalytic mechanism with isoorotate decarboxylase (IDCase) that catalyzes decarboxylation of 5caU to U in fungi. We report here the structures of wild-type and mutant IDCases from Cordyceps militaris and Metarhizium anisopliae in apo form or in complexes with 5caU, U, and an inhibitor 5-nitro-uracil. IDCases adopt a typical (beta/alpha)8 barrel fold of the amidohydrolase superfamily and function as dimers. A Zn2+ is bound at the active site and coordinated by four strictly conserved residues, one Asp and three His. The substrate is recognized by several strictly conserved residues. The functional roles of the key residues at the active site are validated by mutagenesis and biochemical studies. Based on the structural and biochemical data, we present for the first time a novel catalytic mechanism of decarboxylation for IDCases, which might also apply to other members of the amidohydrolase superfamily. In addition, our biochemical data show that IDCases can catalyze decarboxylation of 5caC to C albeit with weak activity, which is the first in vitro evidence for direct decarboxylation of 5caC to C by an enzyme. These findings are valuable in the identification of potential DNA decarboxylase in mammals.Cell Research advance online publication 6 August 2013; doi:10.1038/cr.2013.107.

Crystal structures of isoorotate decarboxylases reveal a novel catalytic mechanism of 5-carboxyl-uracil decarboxylation and shed light on the search for DNA decarboxylase.,Xu S, Li W, Zhu J, Wang R, Li Z, Xu GL, Ding J Cell Res. 2013 Aug 6. doi: 10.1038/cr.2013.107. PMID:23917530<ref>PMID:23917530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hk5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Cordyceps militaris]]
[[Category: Large Structures]]
[[Category: Ding J]]
[[Category: Xu S]]
[[Category: Zhu J]]