Undecaprenyl pyrophosphate synthase

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<StructureSection load='1x07' size='450' side='right' caption='Structure of E. coli UPP complex with isopentenyl pyrophosphate, phosphate and Mg+2 (green) (PDB code [[1x07]]).' scene='59/591995/Cv/4' pspeed='8'>
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<StructureSection load='1x07' size='350' side='right' caption='Structure of E. coli UPP complex with isopentenyl pyrophosphate, phosphate and Mg+2 (green) (PDB code [[1x07]]).' scene='59/591995/Cv/4' pspeed='8'>
== Function ==
== Function ==
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'''Undecaprenyl pyrophosphate synthase''' (UPP) catalyzes the consecutive condensation of farnesyl pyrophosphate (FPP) with 8 molecules of isopentenyl pyrophosphate (IPP) to produce undecaprenyl pyrophosphate. Undecaprenyl pyrophosphate serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall<ref>PMID:15788389</ref>. Bisphosphonate drugs are UPP inhibitors.
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'''Undecaprenyl pyrophosphate synthase''' or '''isoprenyl transferase''' or '''poly-cis-prenyltransferase''' or '''ditrans,polycis-undecaprenyl pyrophosphate synthase ((2E,6E) farnesyl diphosphate specific)''' (UPPS) catalyzes the consecutive condensation of farnesyl pyrophosphate (FPP) with 8 molecules of isopentenyl pyrophosphate (IPP) to produce undecaprenyl pyrophosphate. Undecaprenyl pyrophosphate serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall<ref>PMID:15788389</ref>. '''UPPS''' or '''NUS1''' is a subunit of ''cis''-prenyltransferase<ref>PMID:27402831</ref>. Bisphosphonate drugs are UPP inhibitors.
== Relevance ==
== Relevance ==
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UPP inhibitors are investigated as potential antibacterials<ref>PMID:26718796</ref>.
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UPPS inhibitors are investigated as potential antibacterials<ref>PMID:26718796</ref>.
== Structural highlights ==
== Structural highlights ==
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The <scene name='59/591995/Cv/3'>active site</scene> of UPP contains an <scene name='59/591995/Cv/1'>octahedrally coordinated Mg+2 ion bound to the pyrophosphate group of isopentenyl pyrophosphate</scene><ref>PMID:15788389</ref>. Water molecules shown as red spheres.
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The <scene name='59/591995/Cv/5'>active site</scene> of UPPS (water molecules are shown as red spheres) contains an <scene name='59/591995/Cv/6'>octahedrally coordinated Mg+2 ion bound to the pyrophosphate group of isopentenyl pyrophosphate</scene><ref>PMID:15788389</ref>.
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</StructureSection>
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==3D structures of undecaprenyl pyrophosphate synthase==
==3D structures of undecaprenyl pyrophosphate synthase==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[Undecaprenyl pyrophosphate synthase 3D structures]]
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Undecaprenyl pyrophosphate synthase
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**[[1f75]] – UPP (mutant) – ''Micrococcus luteus''<br />
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**[[3qas]], [[5cqb]] – EcUPP – ''Escherichia coli''<br />
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**[[1jp3]] – EcUPP (mutant) <br />
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**[[2d2r]] – HpUPP (mutant) – ''Helicobacter pylori''<br />
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**[[2vg4]] – MtUPP – ''Mycobacterium tuberculosis''<br />
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**[[5kh2]] – SpUPP – ''Streptococcus pneumoniae''<br />
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*Undecaprenyl pyrophosphate synthase complexes
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**[[1ueh]] – EcUPP + Mg + SO4 + triton<br />
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**[[1v7u]] – EcUPP + FPP <br />
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**[[1x06]] – EcUPP + Mg + FPP analog + IPP<br />
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**[[1x08]] – EcUPP (mutant) + Mg + FPP analog + IPP<br />
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**[[1x07]] – EcUPP + Mg + PO4 + IPP<br />
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**[[1x09]] – EcUPP (mutant) + Mg + IPP<br />
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**[[2e98]], [[2e99]], [[2e9a]], [[2e9c]], [[2e9d]], [[3th8]], [[3sgt]], [[3sgv]], [[3sgx]], [[3sh0]], [[4h2j]], [[4h2m]], [[4h2o]], [[4h38]], [[4h3c]], [[4h3a]], [[4h8e]], [[3wyj]] – EcUPP + bisphosphonate<br />
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**[[5cqj]] – EcUPP + inhibitor <br />
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**[[5kh4]] – SpUPP + FPP <br />
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**[[5kh5]] – SpUPP + inhibitor <br />
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**[[2dtn]] – HpUPP + pyrophosphate<br />
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**[[3ugs]] - UPP + FPP analog – ''Campylobacter jejuni''<br />
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**[[2vg2]] – MtUPP + Pi + PPi + methyl butenyl diphosphate <br />
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**[[2vg3]] – MtUPP + Pi + Mg + geranyl diphosphate <br />
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}}
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of E. coli UPP complex with isopentenyl pyrophosphate, phosphate and Mg+2 (green) (PDB code 1x07).

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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