4PPM

Crystal structure of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14

4PPM の概要

• エントリーDOI: 10.2210/pdb4ppm/pdb
• 分子名称: Aminotransferase, MAGNESIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: transaminase, transferase
• 由来する生物種: Serratia sp. FS14
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 189402.66

構造登録者

Lou, X.D.,Ran, T.T.,Xu, D.Q.,Wang, W.W. (登録日: 2014-02-27, 公開日: 2015-01-14, 最終更新日: 2025-03-26)

主引用文献

Lou, X.D.,Ran, T.T.,Han, N.,Gao, Y.,He, J.,Tang, L.,Xu, D.Q.,Wang, W.W.
Crystal structure of the catalytic domain of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14
Biochem.Biophys.Res.Commun., 447:178-183, 2014

PubMed Abstract: Prodigiosin, a tripyrrole red pigment synthesized by Serratia and some other microbes through a bifurcated biosynthesis pathway, MBC (4-methoxy-2,2'-bipyrrole-5-carbaldehyde) and MAP (2-methyl-3-n-amyl-pyrrole) are synthesized separately and then condensed by PigC to form prodigiosin. MAP is synthesized sequentially by PigD, PigE and PigB. PigE catalyzes the transamination of an amino group to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to form H2MAP. Here we report the crystal structure of the catalytic domain of PigE which involved in the biosynthesis of prodigiosin precursor MAP for the first time to a resolution of 2.3Å with a homodimer in the asymmetric unit. The monomer of PigE catalytic domain is composed of three domains with PLP as cofactor: a small N-terminal domain connecting the catalytic domain with the front part of PigE, a large PLP-binding domain and a C-terminal domain. The residues from both monomers build the PLP binding site at the interface of the dimer which resembles the other PLP-dependent enzymes. Structural comparison of PigE with Thermus thermophilus AcOAT showed a higher hydrophobic and smaller active site of PigE, these differences may be the reason for substrate specificity.

PubMed: 24704447
DOI: 10.1016/j.bbrc.2014.03.125

実験手法

X-RAY DIFFRACTION (2.3 Å)