4huz
From Proteopedia
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| - | + | ==2,6-Dichloro-p-hydroquinone 1,2-Dioxygenase== | |
| - | ===2,6- | + | <StructureSection load='4huz' size='340' side='right' caption='[[4huz]], [[Resolution|resolution]] 2.60Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4huz]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HUZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46429 Sphingobium chlorophenolicum])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4huz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4huz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4huz RCSB], [http://www.ebi.ac.uk/pdbsum/4huz PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Sphingobium chlorophenolicum]] | [[Category: Sphingobium chlorophenolicum]] | ||
| - | [[Category: Green, A R | + | [[Category: Green, A R]] |
| - | [[Category: Hayes, R P | + | [[Category: Hayes, R P]] |
| - | [[Category: Kang, C | + | [[Category: Kang, C]] |
| - | [[Category: Lewis, K M | + | [[Category: Lewis, K M]] |
| - | [[Category: Nissen, M S | + | [[Category: Nissen, M S]] |
| - | [[Category: Xun, L | + | [[Category: Xun, L]] |
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 12:45, 4 January 2015
2,6-Dichloro-p-hydroquinone 1,2-Dioxygenase
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