From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2e1t.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2e1t.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2e1t| PDB=2e1t | SCENE= }} | | {{STRUCTURE_2e1t| PDB=2e1t | SCENE= }} |
| | | | |
| - | '''Crystal structure of Dendranthema morifolium DmAT complexed with malonyl-CoA'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17383962}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17383962 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17383962}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Dmat]] | | [[Category: Dmat]] |
| | [[Category: Malonyl-coa complex]] | | [[Category: Malonyl-coa complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:46:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:56:15 2008'' |
Revision as of 05:56, 28 July 2008
Template:STRUCTURE 2e1t
Crystal structure of Dendranthema morifolium DmAT complexed with malonyl-CoA
Template:ABSTRACT PUBMED 17383962
About this Structure
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 Mon Jul 28 08:56:15 2008
