Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/100301
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Type: Journal article
Title: Crystallization and preliminary crystallographic analysis of defective pollen wall (DPW) protein from Oryza sativa
Author: Wang, W.
Ma, Y.
Suo, Y.
Yan, L.
Zhang, D.
Miao, C.
Citation: Acta Crystallographica Section F:Structural Biology Communications, 2014; 70(6):758-760
Publisher: Wiley
Issue Date: 2014
ISSN: 2053-230X
2053-230X
Statement of
Responsibility: 
Wei Wang, Yuanyuan Ma, Yang Suo, Liming Yan, Dabing Zhang, and Chen Miao
Abstract: The defective pollen wall (dpw) gene of Oryza sativa encodes a fatty acid reductase (DPW) which plays important roles in primary fatty alcohol synthesis. DPW catalyzes the synthesis of 1-hexadecanol. The enzyme shows a higher specificity for palmitoyl-ACP than for palmitoyl-CoA as the substrate, and can only use NADPH as the cofactor. To gain an understanding of the molecular mechanism underlying the reaction catalyzed by DPW, the gene encoding DPW without the N-terminal 80 amino acids (DPWΔ80) was cloned into pET-28a vector and was overexpressed in Escherichia coli. DPWΔ80 was purified to homogeneity and screened for crystallization. DPWΔ80 in complex with NADPH produced crystals that diffracted X-rays to a resolution of 3.4 Å. The crystals belonged to space group P6₁ or P6₅, with unit-cell parameters a=b=222.8, c=114.0 Å, α=β=90, γ=120°.
Keywords: Pollen; Plant Proteins; Crystallization; Oryza
Rights: © 2014 International Union of Crystallography
RMID: 0030023431
DOI: 10.1107/S2053230X14008486
Appears in Collections:Agriculture, Food and Wine publications

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