2A3L
X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate
Summary for 2A3L
| Entry DOI | 10.2210/pdb2a3l/pdb |
| Descriptor | AMP deaminase, ZINC ION, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | atampd, at2g38280, adenosine 5'-monophosphate deaminase, coformycin 5'-phosphate, structural genomics, protein structure initiative, psi, cesg, center for eukaryotic structural genomics, hydrolase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 80934.41 |
| Authors | Han, B.W.,Wesenberg, G.E.,Phillips Jr., G.N.,Bitto, E.,Bingman, C.A.,Allard, S.T.M.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2005-06-25, release date: 2005-07-19, Last modification date: 2024-04-03) |
| Primary citation | Han, B.W.,Bingman, C.A.,Mahnke, D.K.,Bannen, R.M.,Bednarek, S.Y.,Sabina, R.L.,Phillips, G.N. Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1). J.Biol.Chem., 281:14939-14947, 2006 Cited by PubMed Abstract: 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. PubMed: 16543243DOI: 10.1074/jbc.M513009200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.34 Å) |
Structure validation
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