2a3l

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|PDB= 2a3l |SIZE=350|CAPTION= <scene name='initialview01'>2a3l</scene>, resolution 3.34&Aring;
|PDB= 2a3l |SIZE=350|CAPTION= <scene name='initialview01'>2a3l</scene>, resolution 3.34&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=CF5:COFORMYCIN 5&#39;-PHOSPHATE'>CF5</scene>
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|LIGAND= <scene name='pdbligand=CF5:COFORMYCIN+5&#39;-PHOSPHATE'>CF5</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= At2g38280 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
|GENE= At2g38280 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd01319 AMPD]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a3l OCA], [http://www.ebi.ac.uk/pdbsum/2a3l PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2a3l RCSB]</span>
}}
}}
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[[Category: Jr., G N.Phillips.]]
[[Category: Jr., G N.Phillips.]]
[[Category: Wesenberg, G E.]]
[[Category: Wesenberg, G E.]]
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[[Category: CF5]]
 
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[[Category: PO4]]
 
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[[Category: ZN]]
 
[[Category: adenosine 5'-monophosphate deaminase]]
[[Category: adenosine 5'-monophosphate deaminase]]
[[Category: at2g38280]]
[[Category: at2g38280]]
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:34:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:19:31 2008''

Revision as of 04:19, 26 March 2008


PDB ID 2a3l

Drag the structure with the mouse to rotate
, resolution 3.34Å
Ligands: , ,
Gene: At2g38280 (Arabidopsis thaliana)
Domains: AMPD
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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