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

ABSTRACT: AntE from Streptomyces sp. NRRL 2288 is a crotonyl-CoA carboxylase/reductase that catalyzes the reductive carboxylation of various ?,?-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 I2?2?2?, with unit-cell parameters a=76.4, b=96.7, c=129.6?Å, ?=?=?=90.0°. A diffraction data set was collected at the KEK Photon Factory to 2.29?Å resolution.

SUBMITTER: Zhang L

PROVIDER: S-EPMC4051525 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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

Zhang Lihan L Chen Jing J Mori Takahiro T Yan Yan Y Liu Wen W Abe Ikuro I

Acta crystallographica. Section F, Structural biology communications 20140510 Pt 6

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 collecte ...[more]

PMID: 24915081

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