2a3l

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(New page: 200px<br /><applet load="2a3l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a3l, resolution 3.34&Aring;" /> '''X-Ray Structure of A...)
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[[Image:2a3l.gif|left|200px]]<br /><applet load="2a3l" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2a3l, resolution 3.34&Aring;" />
caption="2a3l, resolution 3.34&Aring;" />
'''X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate'''<br />
'''X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate'''<br />
==Overview==
==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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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==
==About this Structure==
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2A3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with ZN, PO4 and CF5 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A3L OCA].
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2A3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=CF5:'>CF5</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A3L OCA].
==Reference==
==Reference==
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Allard, S.T.M.]]
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[[Category: Allard, S T.M.]]
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[[Category: Bingman, C.A.]]
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[[Category: Bingman, C A.]]
[[Category: Bitto, E.]]
[[Category: Bitto, E.]]
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[[Category: CESG, Center.for.Eukaryotic.Structural.Genomics.]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Han, B.W.]]
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[[Category: Han, B W.]]
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[[Category: Jr., G.N.Phillips.]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: Wesenberg, G.E.]]
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[[Category: Wesenberg, G E.]]
[[Category: CF5]]
[[Category: CF5]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:53:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:20 2008''

Revision as of 14:23, 21 February 2008


2a3l, resolution 3.34Å

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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 with , and as ligands. 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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