2a3l

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spinqualitylabelsall models 2a3l, resolution 3.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate

Overview

Embryonic factor 1 (FAC1) is one of the earliest expressed plant genes and, encodes an AMP deaminase (AMPD), which is also an identified herbicide, target. This report identifies an N-terminal transmembrane domain in, Arabidopsis FAC1, explores subcellular fractionation, and presents a 3.3-A, globular catalytic domain x-ray crystal structure with a bound, herbicide-based transition state inhibitor that provides the first glimpse, of a complete AMPD active site. FAC1 contains an (alpha/beta)(8)-barrel, characterized by loops in place of strands 5 and 6 that places it in a, small subset of the amidohydrolase superfamily with imperfect folds., Unlike tetrameric animal orthologs, FAC1 is a dimer and each subunit, contains an exposed Walker A motif that may be involved in the dramatic, combined K(m) (25-80-fold lower) and V(max) (5-6-fold higher) activation, by ATP. Normal mode analysis predicts a hinge motion that flattens basic, surfaces on each monomer that flank the dimer interface, which suggests a, reversible association between the FAC1 globular catalytic domain and, intracellular membranes, with N-terminal transmembrane and disordered, linker regions serving as the anchor and attachment to the globular, catalytic domain, respectively.

About this Structure

2A3L is a Single protein structure of sequence from Arabidopsis thaliana with ZN, PO4 and CF5 as ligands. Full crystallographic information is available from OCA.

Reference

Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1)., Han BW, Bingman CA, Mahnke DK, Bannen RM, Bednarek SY, Sabina RL, Phillips GN Jr, J Biol Chem. 2006 May 26;281(21):14939-47. Epub 2006 Mar 16. PMID:16543243

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