M. luteus B-P 26 heterodimeric hexaprenyl diphosphate synthase in complex with magnesium and FPP analogueM. luteus B-P 26 heterodimeric hexaprenyl diphosphate synthase in complex with magnesium and FPP analogue

Structural highlights

3aqc is a 4 chain structure with sequence from Micrococcus luteus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.61Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HEXA_MICLU Catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. Large subunit Hexs-B catalyzes the condensation reaction and the final product chain length is cooperatively regulated by both the Hexs-A and Hexs-B subunits using the whole size of the hydrophobic cleft as a ruler.[1] [2] [3]

References

  1. Nagaki M, Kimura K, Kimura H, Maki Y, Goto E, Nishino T, Koyama T. Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases. Bioorg Med Chem Lett. 2001 Aug 20;11(16):2157-9. PMID:11514159
  2. Fujii H, Koyama T, Ogura K. Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components. J Biol Chem. 1982 Dec 25;257(24):14610-2. PMID:7174655
  3. Shimizu N, Koyama T, Ogura K. Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase. J Bacteriol. 1998 Mar;180(6):1578-81. PMID:9515931

3aqc, resolution 2.61Å

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