Undecaprenyl pyrophosphate synthase: Difference between revisions
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<StructureSection load='1x07' size=' | <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 == | ||
'''Undecaprenyl pyrophosphate synthase''' ( | '''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 == | ||
UPPS inhibitors are investigated as potential antibacterials<ref>PMID:26718796</ref>. | |||
== Structural highlights == | == Structural highlights == | ||
The active site of | 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>. | ||
==3D structures of undecaprenyl pyrophosphate synthase== | ==3D structures of undecaprenyl pyrophosphate synthase== | ||
[[Undecaprenyl pyrophosphate synthase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
</StructureSection> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] |