2e1v
From Proteopedia
(New page: 200px<br /><applet load="2e1v" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e1v, resolution 1.80Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | The BAHD family is a class of acyl-CoA-dependent acyltransferases | + | The BAHD family is a class of acyl-CoA-dependent acyltransferases that are involved in plant secondary metabolism and show a diverse range of specificities for acyl acceptors. Anthocyanin acyltransferases make up an important class of the BAHD family and catalyze the acylation of anthocyanins that are responsible for most of the red-to-blue colors of flowers. Here, we describe crystallographic and mutational studies of three similar anthocyanin malonyltransferases from red chrysanthemum petals: anthocyanidin 3-O-glucoside-6''-O-malonyltransferase (Dm3MaT1), anthocyanidin 3-O-glucoside-3'', 6''-O-dimalonyltransferase (Dm3MaT2), and a homolog (Dm3MaT3). Mutational analyses revealed that seven amino acid residues in the N- and C-terminal regions are important for the differential acyl-acceptor specificity between Dm3MaT1 and Dm3MaT2. Crystallographic studies of Dm3MaT3 provided the first structure of a BAHD member, complexed with acyl-CoA, showing the detailed interactions between the enzyme and acyl-CoA molecules. The structure, combined with the results of mutational analyses, allowed us to identify the acyl-acceptor binding site of anthocyanin malonyltransferases, which is structurally different from the corresponding portion of vinorine synthase, another BAHD member, thus permitting the diversity of the acyl-acceptor specificity of BAHD family to be understood. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structural and mutational studies of anthocyanin malonyltransferases establish the features of BAHD enzyme catalysis., Unno H, Ichimaida F, Suzuki H, Takahashi S, Tanaka Y, Saito A, Nishino T, Kusunoki M, Nakayama T, J Biol Chem. 2007 Mar 23 | + | Structural and mutational studies of anthocyanin malonyltransferases establish the features of BAHD enzyme catalysis., Unno H, Ichimaida F, Suzuki H, Takahashi S, Tanaka Y, Saito A, Nishino T, Kusunoki M, Nakayama T, J Biol Chem. 2007 May 25;282(21):15812-22. Epub 2007 Mar 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17383962 17383962] |
[[Category: Chrysanthemum x morifolium]] | [[Category: Chrysanthemum x morifolium]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: seleno-methionine derivative]] | [[Category: seleno-methionine derivative]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:05:02 2008'' |
Revision as of 15:05, 21 February 2008
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Crystal structure of Dendranthema morifolium DmAT, seleno-methionine derivative
Overview
The BAHD family is a class of acyl-CoA-dependent acyltransferases that are involved in plant secondary metabolism and show a diverse range of specificities for acyl acceptors. Anthocyanin acyltransferases make up an important class of the BAHD family and catalyze the acylation of anthocyanins that are responsible for most of the red-to-blue colors of flowers. Here, we describe crystallographic and mutational studies of three similar anthocyanin malonyltransferases from red chrysanthemum petals: anthocyanidin 3-O-glucoside-6-O-malonyltransferase (Dm3MaT1), anthocyanidin 3-O-glucoside-3, 6-O-dimalonyltransferase (Dm3MaT2), and a homolog (Dm3MaT3). Mutational analyses revealed that seven amino acid residues in the N- and C-terminal regions are important for the differential acyl-acceptor specificity between Dm3MaT1 and Dm3MaT2. Crystallographic studies of Dm3MaT3 provided the first structure of a BAHD member, complexed with acyl-CoA, showing the detailed interactions between the enzyme and acyl-CoA molecules. The structure, combined with the results of mutational analyses, allowed us to identify the acyl-acceptor binding site of anthocyanin malonyltransferases, which is structurally different from the corresponding portion of vinorine synthase, another BAHD member, thus permitting the diversity of the acyl-acceptor specificity of BAHD family to be understood.
About this Structure
2E1V is a Protein complex structure of sequences from Chrysanthemum x morifolium. Full crystallographic information is available from OCA.
Reference
Structural and mutational studies of anthocyanin malonyltransferases establish the features of BAHD enzyme catalysis., Unno H, Ichimaida F, Suzuki H, Takahashi S, Tanaka Y, Saito A, Nishino T, Kusunoki M, Nakayama T, J Biol Chem. 2007 May 25;282(21):15812-22. Epub 2007 Mar 23. PMID:17383962
Page seeded by OCA on Thu Feb 21 17:05:02 2008
