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4k22

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==Structure of the C-terminal truncated form of E.Coli C5-hydroxylase UBII involved in ubiquinone (Q8) biosynthesis==
==Structure of the C-terminal truncated form of E.Coli C5-hydroxylase UBII involved in ubiquinone (Q8) biosynthesis==
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<StructureSection load='4k22' size='340' side='right' caption='[[4k22]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4k22' size='340' side='right'caption='[[4k22]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4k22]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K22 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4k22]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K22 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">visC, b2906, JW2874 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<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=4k22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k22 RCSB], [http://www.ebi.ac.uk/pdbsum/4k22 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k22 OCA], [https://pdbe.org/4k22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k22 RCSB], [https://www.ebi.ac.uk/pdbsum/4k22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k22 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/UBII_ECOLI UBII_ECOLI] FAD-dependent monooxygenase required for the aerobic hydroxylation of 2-octaprenylphenol to 2-octaprenyl-6-hydroxy-phenol, the first hydroxylation step in coenzyme Q (ubiquinone) biosynthesis.<ref>PMID:23709220</ref>
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Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic and biochemical experiments, we establish that the UbiI protein functions in the C5-hydroxylation reaction. A strain deficient in ubiI has a low level of Q and accumulates a compound derived from the Q biosynthetic pathway, which we purified and characterized. We also demonstrate that UbiI is only implicated in aerobic Q biosynthesis and that an alternative enzyme catalyzes the C5-hydroxylation reaction in the absence of oxygen. We have solved the crystal structure of a truncated form of UbiI. This structure shares many features with the canonical FAD-dependent para-hydroxybenzoate hydroxylase and represents the first structural characterization of a monooxygenase involved in Q biosynthesis. Site-directed mutagenesis confirms that residues of the flavin binding pocket of UbiI are important for activity. With our identification of UbiI, the three monooxygenases necessary for aerobic Q biosynthesis in E. coli are known.
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ubiI, a New Gene in Escherichia coli Coenzyme Q Biosynthesis, Is Involved in Aerobic C5-hydroxylation.,Hajj Chehade M, Loiseau L, Lombard M, Pecqueur L, Ismail A, Smadja M, Golinelli-Pimpaneau B, Mellot-Draznieks C, Hamelin O, Aussel L, Kieffer-Jaquinod S, Labessan N, Barras F, Fontecave M, Pierrel F J Biol Chem. 2013 Jul 5;288(27):20085-92. doi: 10.1074/jbc.M113.480368. Epub 2013, May 24. PMID:23709220<ref>PMID:23709220</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli k-12]]
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[[Category: Escherichia coli K-12]]
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[[Category: Fontecave, M]]
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[[Category: Large Structures]]
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[[Category: Golinelli-pimpaneau, B]]
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[[Category: Fontecave M]]
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[[Category: Lombard, M]]
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[[Category: Golinelli-pimpaneau B]]
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[[Category: Pecqueur, L]]
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[[Category: Lombard M]]
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[[Category: Hydroxylase]]
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[[Category: Pecqueur L]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

Structure of the C-terminal truncated form of E.Coli C5-hydroxylase UBII involved in ubiquinone (Q8) biosynthesis

PDB ID 4k22

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