2a3l: Difference between revisions

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[[Image:2a3l.gif|left|200px]]
{{Seed}}
[[Image:2a3l.png|left|200px]]


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{{STRUCTURE_2a3l|  PDB=2a3l  |  SCENE=  }}  
{{STRUCTURE_2a3l|  PDB=2a3l  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_16543243}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16543243 16543243]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16543243 16543243]
Crystallization and preliminary X-ray crystallographic analysis of adenosine 5'-monophosphate deaminase (AMPD) from Arabidopsis thaliana in complex with coformycin 5'-phosphate., Han BW, Bingman CA, Mahnke DK, Sabina RL, Phillips GN Jr, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Aug 1;61(Pt, 8):740-2. Epub 2005 Jul 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511144 16511144]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Psi]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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