3NPE

Structure of VP14 in complex with oxygen

Summary for 3NPE

• Entry DOI: 10.2210/pdb3npe/pdb
• Descriptor: 9-cis-epoxycarotenoid dioxygenase 1, chloroplastic, FE (II) ION, OXYGEN MOLECULE, ... (6 entities in total)
• Functional Keywords: dioxygenase, seven blade beta propeller, abscisic acid, non heme iron, oxidoreductase
• Biological source: Zea mays (maize)
• Cellular location: Plastid, chloroplast stroma : O24592
• Total number of polymer chains: 1
• Total formula weight: 58016.01

Authors

Messing, S.A.,Gabelli, S.B.,Amzel, L.M. (deposition date: 2010-06-28, release date: 2010-11-10, Last modification date: 2024-11-20)

Primary citation

Messing, S.A.,Gabelli, S.B.,Echeverria, I.,Vogel, J.T.,Guan, J.C.,Tan, B.C.,Klee, H.J.,McCarty, D.R.,Amzel, L.M.
Structural insights into maize viviparous14, a key enzyme in the biosynthesis of the phytohormone abscisic acid.
Plant Cell, 22:2970-2980, 2010

PubMed Abstract: The key regulatory step in the biosynthesis of abscisic acid (ABA), a hormone central to the regulation of several important processes in plants, is the oxidative cleavage of the 11,12 double bond of a 9-cis-epoxycarotenoid. The enzyme viviparous14 (VP14) performs this cleavage in maize (Zea mays), making it a target for the rational design of novel chemical agents and genetic modifications that improve plant behavior through the modulation of ABA levels. The structure of VP14, determined to 3.2-Å resolution, provides both insight into the determinants of regio- and stereospecificity of this enzyme and suggests a possible mechanism for oxidative cleavage. Furthermore, mutagenesis of the distantly related CCD1 of maize shows how the VP14 structure represents a template for all plant carotenoid cleavage dioxygenases (CCDs). In addition, the structure suggests how VP14 associates with the membrane as a way of gaining access to its membrane soluble substrate.

PubMed: 20884803
DOI: 10.1105/tpc.110.074815

Experimental method

X-RAY DIFFRACTION (3.2 Å)