PDBsum entry 2e1v

Transferase

PDB id: 2e1v

Contents

Protein chains

440 a.a. *

Waters ×946

* Residue conservation analysis

PDB id:

2e1v

Name:

Transferase

Title:

Crystal structure of dendranthema morifolium dmat, seleno-methionine derivative

Structure:

Acyl transferase. Chain: a, b. Engineered: yes

Source:

Chrysanthemum x morifolium. Organism_taxid: 41568. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å R-factor: 0.198 R-free: 0.234

Authors:

H.Unno,F.Ichimaida,M.Kusunoki,T.Nakayama

Key ref:

H.Unno et al. (2007). Structural and mutational studies of anthocyanin malonyltransferases establish the features of BAHD enzyme catalysis. J Biol Chem, 282, 15812-15822. PubMed id: 17383962 DOI: 10.1074/jbc.M700638200

Date:

28-Oct-06 Release date: 10-Apr-07

Protein chains

A4PHY4  (A4PHY4_CHRMO) -  Anthocyanin malonyltransferase homolog from Chrysanthemum morifolium

Seq: 454 a.a.

Struc: 440 a.a.

Enzyme reactions

• Enzyme class: E.C.2.-.-.-

DOI no: 10.1074/jbc.M700638200

J Biol Chem 282:15812-15822 (2007)

PubMed id: 17383962

Structural and mutational studies of anthocyanin malonyltransferases establish the features of BAHD enzyme catalysis.

H.Unno, F.Ichimaida, H.Suzuki, S.Takahashi, Y.Tanaka, A.Saito, T.Nishino, M.Kusunoki, T.Nakayama.

ABSTRACT

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.

Selected figure(s)

Figure 1.
FIGURE 1. Malonyltransferase activities of Dm3MaT1, Dm3MaT2, and Dm3MaT3 from red chrysanthemum petals. The names of the substrates for 3MaT1 activity are pelargonidin 3-O-glucoside (R[1] = R[2] = -H), cyanidin 3-O-glucoside (R[1] = -OH, R[2] = -H), and delphinidin 3-O-glucoside (R[1] = R[2] = -OH) (1). Substrates for 3MaT2 activity (2) and the product (3) are collectively referred to as anthocyanidin 3-O-6''-O-malonylglucoside and anthocyanidin 3-O-3'',6''-O-dimalonylglucoside, respectively. The structures of the anthocyanins are shown as their flavylium forms. Key positional numberings are labeled on 1.

Figure 4.
FIGURE 4. Surface diagram showing the front face (A) and the back face (B) of Dm3MaT3. The coordinates shown as sticks are for bound malonyl-CoA. This figure was created with PyMOL program (18). The location in Dm3MaT3 of amino acid residues that correspond to those important for the 3MaT2 activity of Dm3MaT2 revealed by mutational studies are shown in green. C, a close-up view of the acyl-acceptor binding pocket.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 15812-15822) copyright 2007.

Figures were selected by an automated process.