3b6z

Lovastatin polyketide enoyl reductase (LovC) complexed with 2'-phosphoadenosyl isomer of crotonoyl-CoALovastatin polyketide enoyl reductase (LovC) complexed with 2'-phosphoadenosyl isomer of crotonoyl-CoA

Structural highlights

3b6z is a 1 chain structure with sequence from Aspergillus terreus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.88Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LOVC_ASPTE Catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the LovB-mediated biosynthesis of the lovastatin nonaketide chain.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Kennedy J, Auclair K, Kendrew SG, Park C, Vederas JC, Hutchinson CR. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science. 1999 May 21;284(5418):1368-72. PMID:10334994
↑ Ma SM, Li JW, Choi JW, Zhou H, Lee KK, Moorthie VA, Xie X, Kealey JT, Da Silva NA, Vederas JC, Tang Y. Complete reconstitution of a highly reducing iterative polyketide synthase. Science. 2009 Oct 23;326(5952):589-92. doi: 10.1126/science.1175602. PMID:19900898 doi:http://dx.doi.org/10.1126/science.1175602
↑ Ames BD, Nguyen C, Bruegger J, Smith P, Xu W, Ma S, Wong E, Wong S, Xie X, Li JW, Vederas JC, Tang Y, Tsai SC. Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis. Proc Natl Acad Sci U S A. 2012 Jun 25. PMID:22733743 doi:10.1073/pnas.1113029109

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OCA

[1] Kennedy J, Auclair K, Kendrew SG, Park C, Vederas JC, Hutchinson CR. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science. 1999 May 21;284(5418):1368-72. PMID:10334994

[2] Ma SM, Li JW, Choi JW, Zhou H, Lee KK, Moorthie VA, Xie X, Kealey JT, Da Silva NA, Vederas JC, Tang Y. Complete reconstitution of a highly reducing iterative polyketide synthase. Science. 2009 Oct 23;326(5952):589-92. doi: 10.1126/science.1175602. PMID:19900898 doi:http://dx.doi.org/10.1126/science.1175602

[3] Ames BD, Nguyen C, Bruegger J, Smith P, Xu W, Ma S, Wong E, Wong S, Xie X, Li JW, Vederas JC, Tang Y, Tsai SC. Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis. Proc Natl Acad Sci U S A. 2012 Jun 25. PMID:22733743 doi:10.1073/pnas.1113029109

[1]

[2]

[3]

3b6z

Lovastatin polyketide enoyl reductase (LovC) complexed with 2'-phosphoadenosyl isomer of crotonoyl-CoALovastatin polyketide enoyl reductase (LovC) complexed with 2'-phosphoadenosyl isomer of crotonoyl-CoA

Structural highlights

Function

Evolutionary Conservation

References

Contents

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3b6z

Lovastatin polyketide enoyl reductase (LovC) complexed with 2'-phosphoadenosyl isomer of crotonoyl-CoALovastatin polyketide enoyl reductase (LovC) complexed with 2'-phosphoadenosyl isomer of crotonoyl-CoA

Structural highlights

Function

Evolutionary Conservation

References

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