Crystallization and preliminary X-ray diffraction analysis of AntE, a crotonyl-CoA carboxylase/reductase from Streptomyces sp. NRRL 2288

Lihan Zhang; Jing Chen; Takahiro Mori; Yan Yan; Wen Liu; Ikuro Abe

doi:10.1107/S2053230X14008371

Crystallization and preliminary X-ray diffraction analysis of AntE, a crotonyl-CoA carboxylase/reductase from Streptomyces sp. NRRL 2288

Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):734-7. doi: 10.1107/S2053230X14008371. Epub 2014 May 10.

Authors

Lihan Zhang¹, Jing Chen¹, Takahiro Mori¹, Yan Yan², Wen Liu², Ikuro Abe¹

Affiliations

¹ Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
² State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, People's Republic of China.

Abstract

AntE from Streptomyces sp. NRRL 2288 is a crotonyl-CoA carboxylase/reductase that catalyzes the reductive carboxylation of various α,β-unsaturated acyl-CoAs to provide the building block at the C7 position for antimycin A biosynthesis. Recombinant AntE expressed in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group I222 or I2₁2₁2₁, with unit-cell parameters a=76.4, b=96.7, c=129.6 Å, α=β=γ=90.0°. A diffraction data set was collected at the KEK Photon Factory to 2.29 Å resolution.

Keywords: AntE; Streptomyces sp. NRRL 2288; crotonyl-CoA carboxylase/reductase; polyketide.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acyl-CoA Dehydrogenases / chemistry*
Crystallization
Crystallography, X-Ray
Streptomyces / enzymology*

Substances

Acyl-CoA Dehydrogenases
acyl-CoA dehydrogenase (NADP+)