3npe | pdb_00003npe

Structure of VP14 in complex with oxygen

spinqualitylabelsall models 3npe, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3npe is a 1 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DIO, FE2, OH, OXY Gene: VP14 (Zea mays) Activity: 9-cis-epoxycarotenoid dioxygenase, with EC number 1.13.11.51 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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-A 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. Structural insights into maize viviparous14, a key enzyme in the biosynthesis of the phytohormone abscisic acid.,Messing SA, Gabelli SB, Echeverria I, Vogel JT, Guan JC, Tan BC, Klee HJ, McCarty DR, Amzel LM Plant Cell. 2010 Sep;22(9):2970-80. Epub 2010 Sep 30. PMID:20884803 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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