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2a3l

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{{STRUCTURE_2a3l| PDB=2a3l | SCENE= }}
{{STRUCTURE_2a3l| PDB=2a3l | SCENE= }}
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'''X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate'''
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===X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate===
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==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]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:26:42 2008''

Revision as of 06:26, 28 July 2008

Image:2a3l.png

Template:STRUCTURE 2a3l

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

Template:ABSTRACT PUBMED 16543243

About this Structure

2A3L is a Single protein structure of sequence from Arabidopsis thaliana. 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

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:16511144

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