View source for 4huz


==2,6-Dichloro-p-hydroquinone 1,2-Dioxygenase==
<StructureSection load='4huz' size='340' side='right'caption='[[4huz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4huz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_chlorophenolicum Sphingobium chlorophenolicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HUZ 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=4huz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4huz OCA], [https://pdbe.org/4huz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4huz RCSB], [https://www.ebi.ac.uk/pdbsum/4huz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4huz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9ZBB0_SPHCR Q9ZBB0_SPHCR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PcpA (2,6-dichloro-p-hydroquinone 1,2-dioxygenase) from Sphingobium chlorophenolicum, a non-haem Fe(II) dioxygenase capable of cleaving the aromatic ring of p-hydroquinone and its substituted variants, is a member of the recently discovered p-hydroquinone 1,2-dioxygenases. Here we report the 2.6 A structure of PcpA, which consists of four betaalphabetabetabeta motifs, a hallmark of the vicinal oxygen chelate superfamily. The secondary co-ordination sphere of the Fe(II) centre forms an extensive hydrogen-bonding network with three solvent exposed residues, linking the catalytic Fe(II) to solvent. A tight hydrophobic pocket provides p-hydroquinones access to the Fe(II) centre. The p-hydroxyl group is essential for the substrate-binding, thus phenols and catechols, lacking a p-hydroxyl group, do not bind to PcpA. Site-directed mutagenesis and kinetic analysis confirm the critical catalytic role played by the highly conserved His10, Thr13, His226 and Arg259. Based on these results, we propose a general reaction mechanism for p-hydroquinone 1,2-dioxygenases.

Structural characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) from Sphingobium chlorophenolicum, a new type of aromatic ring-cleavage enzyme.,Hayes RP, Green AR, Nissen MS, Lewis KM, Xun L, Kang C Mol Microbiol. 2013 Mar 14. doi: 10.1111/mmi.12204. PMID:23489289<ref>PMID:23489289</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4huz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sphingobium chlorophenolicum]]
[[Category: Green AR]]
[[Category: Hayes RP]]
[[Category: Kang C]]
[[Category: Lewis KM]]
[[Category: Nissen MS]]
[[Category: Xun L]]