2e1t: Difference between revisions
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'''Crystal structure of Dendranthema morifolium DmAT complexed with malonyl-CoA''' | {{Structure | ||
|PDB= 2e1t |SIZE=350|CAPTION= <scene name='initialview01'>2e1t</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MLC:MALONYL-COENZYME A'>MLC</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of Dendranthema morifolium DmAT complexed with malonyl-CoA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2E1T is a [ | 2E1T is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Chrysanthemum_x_morifolium Chrysanthemum x morifolium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E1T OCA]. | ||
==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 May 25;282(21):15812-22. Epub 2007 Mar 23. PMID:[http:// | 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://www.ncbi.nlm.nih.gov/pubmed/17383962 17383962] | ||
[[Category: Chrysanthemum x morifolium]] | [[Category: Chrysanthemum x morifolium]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: malonyl-coa complex]] | [[Category: malonyl-coa complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:34:11 2008'' | ||
Revision as of 14:34, 20 March 2008
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| 2e1t, resolution 2.10Å | |||||||||||||
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| Ligands: | MLC | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of Dendranthema morifolium DmAT complexed with malonyl-CoA
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
2E1T 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
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