1TFU

phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis

1TFU の概要

• エントリーDOI: 10.2210/pdb1tfu/pdb
• 分子名称: Phosphopantetheine adenylyltransferase (2 entities in total)
• 機能のキーワード: transport protein, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (By similarity): P0A530
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17159.74

構造登録者

Morris, V.K.,Izard, T.,TB Structural Genomics Consortium (TBSGC) (登録日: 2004-05-27, 公開日: 2004-09-14, 最終更新日: 2024-02-14)

主引用文献

Morris, V.K.,Izard, T.
Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Protein Sci., 13:2547-2552, 2004

PubMed Abstract: Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in prokaryotic coenzyme A (CoA) biosynthesis, directing the transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to yield dephospho-CoA (dPCoA). The crystal structures of Escherichia coli PPAT bound to its substrates, product, and inhibitor revealed an allosteric hexameric enzyme with half-of-sites reactivity, and established an in-line displacement catalytic mechanism. To provide insight into the mechanism of ligand binding we solved the apoenzyme (Apo) crystal structure of PPAT from Mycobacterium tuberculosis. In its Apo form, PPAT is a symmetric hexamer with an open solvent channel. However, ligand binding provokes asymmetry and alters the structure of the solvent channel, so that ligand binding becomes restricted to one trimer.

PubMed: 15322293
DOI: 10.1110/ps.04816904

実験手法

X-RAY DIFFRACTION (1.99 Å)