4A0G

Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana in its apo form.

4A0G の概要

• エントリーDOI: 10.2210/pdb4a0g/pdb
• 関連するPDBエントリー: 4A0F 4A0H 4A0R
• 分子名称: ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: transferase, bio3-bio1, biotin synthesis
• 由来する生物種: ARABIDOPSIS THALIANA (THALE CRESS)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 367706.56

構造登録者

Cobessi, D.,Dumas, R.,Pautre, V.,Meinguet, C.,Ferrer, J.L.,Alban, C. (登録日: 2011-09-09, 公開日: 2012-06-13, 最終更新日: 2023-12-20)

主引用文献

Cobessi, D.,Dumas, R.,Pautre, V.,Meinguet, C.,Ferrer, J.L.,Alban, C.
Biochemical and Structural Characterization of the Arabidopsis Bifunctional Enzyme Dethiobiotin Synthetase-Diaminopelargonic Acid Aminotransferase: Evidence for Substrate Channeling in Biotin Synthesis.
Plant Cell, 24:1608-, 2012

PubMed Abstract: Diaminopelargonic acid aminotransferase (DAPA-AT) and dethiobiotin synthetase (DTBS) catalyze the antepenultimate and the penultimate steps, respectively, of biotin synthesis. Whereas DAPA-AT and DTBS are encoded by distinct genes in bacteria, in biotin-synthesizing eukaryotes (plants and most fungi), both activities are carried out by a single enzyme encoded by a bifunctional gene originating from the fusion of prokaryotic monofunctional ancestor genes. In few angiosperms, including Arabidopsis thaliana, this chimeric gene (named BIO3-BIO1) also produces a bicistronic transcript potentially encoding separate monofunctional proteins that can be produced following an alternative splicing mechanism. The functional significance of the occurrence of a bifunctional enzyme in biotin synthesis pathway in eukaryotes and the relative implication of each of the potential enzyme forms (bifunctional versus monofunctional) in the plant biotin pathway are unknown. In this study, we demonstrate that the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both DAPA-AT and DTBS reactions in vitro and is targeted to mitochondria in vivo. Our biochemical and kinetic characterizations of the pure recombinant enzyme show that in the course of the reaction, the DAPA intermediate is directly transferred from the DAPA-AT active site to the DTBS active site. Analysis of several structures of the enzyme crystallized in complex with and without its ligands reveals key structural elements involved for acquisition of bifunctionality and brings, together with mutagenesis experiments, additional evidences for substrate channeling.

PubMed: 22547782
DOI: 10.1105/TPC.112.097675

実験手法

X-RAY DIFFRACTION (2.502 Å)