2a3l
From Proteopedia
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'''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''' | ||
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[[Category: Jr., G N.Phillips.]] | [[Category: Jr., G N.Phillips.]] | ||
[[Category: Wesenberg, G E.]] | [[Category: Wesenberg, G E.]] | ||
- | [[Category: | + | [[Category: Adenosine 5'-monophosphate deaminase]] |
- | [[Category: | + | [[Category: At2g38280]] |
- | [[Category: | + | [[Category: Atampd]] |
- | [[Category: | + | [[Category: Center for eukaryotic structural genomic]] |
- | [[Category: | + | [[Category: Cesg]] |
- | [[Category: | + | [[Category: Coformycin 5'-phosphate]] |
- | [[Category: | + | [[Category: Protein structure initiative]] |
- | [[Category: | + | [[Category: Psi]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:33:24 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:33, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 18:33:24 2008
Categories: Arabidopsis thaliana | Single protein | Allard, S T.M. | Bingman, C A. | Bitto, E. | CESG, Center for Eukaryotic Structural Genomics. | Han, B W. | Jr., G N.Phillips. | Wesenberg, G E. | Adenosine 5'-monophosphate deaminase | At2g38280 | Atampd | Center for eukaryotic structural genomic | Cesg | Coformycin 5'-phosphate | Protein structure initiative | Psi | Structural genomic