4zaf

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==Structure of UbiX in complex with oxidised FMN and dimethylallyl monophosphate==
==Structure of UbiX in complex with oxidised FMN and dimethylallyl monophosphate==
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<StructureSection load='4zaf' size='340' side='right' caption='[[4zaf]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
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<StructureSection load='4zaf' size='340' side='right'caption='[[4zaf]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4zaf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZAF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4zaf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZAF 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=4LR:DIMETHYLALLYL+MONOPHOSPHATE'>4LR</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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]] 1.71&#8491;</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=4zaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zaf OCA], [http://pdbe.org/4zaf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zaf RCSB], [http://www.ebi.ac.uk/pdbsum/4zaf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zaf ProSAT]</span></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=4LR:DIMETHYLALLYL+MONOPHOSPHATE'>4LR</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></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=4zaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zaf OCA], [https://pdbe.org/4zaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zaf RCSB], [https://www.ebi.ac.uk/pdbsum/4zaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zaf 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/UBIX_PSEAE UBIX_PSEAE] Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.[HAMAP-Rule:MF_01984]<ref>PMID:26083743</ref>
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Ubiquinone (also known as coenzyme Q) is a ubiquitous lipid-soluble redox cofactor that is an essential component of electron transfer chains. Eleven genes have been implicated in bacterial ubiquinone biosynthesis, including ubiX and ubiD, which are responsible for decarboxylation of the 3-octaprenyl-4-hydroxybenzoate precursor. Despite structural and biochemical characterization of UbiX as a flavin mononucleotide (FMN)-binding protein, no decarboxylase activity has been detected. Here we report that UbiX produces a novel flavin-derived cofactor required for the decarboxylase activity of UbiD. UbiX acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N5 and C6 atoms. This adds a fourth non-aromatic ring to the flavin isoalloxazine group. In contrast to other prenyltransferases, UbiX is metal-independent and requires dimethylallyl-monophosphate as substrate. Kinetic crystallography reveals that the prenyltransferase mechanism of UbiX resembles that of the terpene synthases. The active site environment is dominated by pi systems, which assist phosphate-C1' bond breakage following FMN reduction, leading to formation of the N5-C1' bond. UbiX then acts as a chaperone for adduct reorientation, via transient carbocation species, leading ultimately to formation of the dimethylallyl C3'-C6 bond. Our findings establish the mechanism for formation of a new flavin-derived cofactor, extending both flavin and terpenoid biochemical repertoires.
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UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis.,White MD, Payne KA, Fisher K, Marshall SA, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Rigby SE, Scrutton NS, Hay S, Leys D Nature. 2015 Jun 25;522(7557):502-6. doi: 10.1038/nature14559. Epub 2015 Jun 17. PMID:26083743<ref>PMID:26083743</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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<div class="pdbe-citations 4zaf" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Leys, D]]
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[[Category: Large Structures]]
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[[Category: White, M D]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Flavin binding]]
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[[Category: Leys D]]
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[[Category: Lyase]]
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[[Category: White MD]]
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[[Category: Prenyl transferase]]
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[[Category: Ubix]]
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Current revision

Structure of UbiX in complex with oxidised FMN and dimethylallyl monophosphate

PDB ID 4zaf

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