2BYD

Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase

2BYD の概要

• エントリーDOI: 10.2210/pdb2byd/pdb
• 分子名称: HSPC223, BROMIDE ION (3 entities in total)
• 機能のキーワード: transferase, fatty acid biosynthesis, phosphopantetheine transferase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38157.44

構造登録者

Bunkoczi, G.,Wu, X.,Dubinina, E.,Johansson, C.,Smee, C.,Turnbull, A.,Oppermann, U.,von Delft, F.,Arrowsmith, C.,Edwards, A.,Sundstrom, M.,Weigelt, J. (登録日: 2005-07-29, 公開日: 2005-08-05, 最終更新日: 2024-05-08)

主引用文献

Bunkoczi, G.,Pasta, S.,Joshi, A.,Wu, X.,Kavanagh, K.L.,Smith, S.,Oppermann, U.
Mechanism and substrate recognition of human holo ACP synthase.
Chem. Biol., 14:1243-1253, 2007

PubMed Abstract: Mammals utilize a single phosphopantetheinyl transferase for the posttranslational modification of at least three different apoproteins: the carrier protein components of cytosolic and mitochondrial fatty acid synthases and the aminoadipate semialdehyde reductase involved in lysine degradation. We determined the crystal structure of the human phosphopantetheinyl transferase, a eukaryotic phosphopantetheinyl transferase characterized, complexed with CoA and Mg(2+), and in ternary complex with CoA and ACP. The involvement of key residues in ligand binding and catalysis was confirmed by mutagenesis and kinetic analysis. Human phosphopantetheinyl transferase exhibits an alpha/beta fold and 2-fold pseudosymmetry similar to the Sfp phosphopantetheinyl transferase from Bacillus subtilis. Although the bound ACP exhibits a typical four-helix structure, its binding is unusual in that it is facilitated predominantly by hydrophobic interactions. A detailed mechanism is proposed describing the substrate binding and catalytic process.

PubMed: 18022563
DOI: 10.1016/j.chembiol.2007.10.013

実験手法

X-RAY DIFFRACTION (2 Å)