4E1A

Phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis at 1.62A resolution

4E1A の概要

• エントリーDOI: 10.2210/pdb4e1a/pdb
• 分子名称: Phosphopantetheine adenylyltransferase, GLYCEROL (3 entities in total)
• 機能のキーワード: 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: 17740.35

構造登録者

Timofeev, V.I.,Smirnova, E.A.,Chupova, L.A.,Esipov, R.S.,Kuranova, I.P. (登録日: 2012-03-06, 公開日: 2012-11-21, 最終更新日: 2024-02-28)

主引用文献

Timofeev, V.,Smirnova, E.,Chupova, L.,Esipov, R.,Kuranova, I.
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction.
Acta Crystallogr.,Sect.D, 68:1660-1670, 2012

PubMed Abstract: Structures of recombinant phosphopantetheine adenylyltransferase (PPAT) from Mycobacterium tuberculosis (PPATMt) in the apo form and in complex with the substrate ATP were determined at 1.62 and 1.70 Å resolution, respectively, using crystals grown in microgravity by the counter-diffusion method. The ATP molecule of the PPATMt-ATP complex was located with full occupancy in the active-site cavity. Comparison of the solved structures with previously determined structures of PPATMt complexed with the reaction product dephosphocoenzyme A (dPCoA) and the feedback inhibitor coenzyme A (CoA) was performed using superposition on C(α) atoms. The peculiarities of the arrangement of the ligands in the active-site cavity of PPATMt are described. The conformational states of the PPAT molecule in the consequent steps of the catalyzed reaction in the apo enzyme and the enzyme-substrate and enzyme-product complexes are characterized. It is shown that the binding of ATP and dPCoA induces the rearrangement of a short part of the polypeptide chain restricting the active-site cavity in the subunits of the hexameric enzyme molecule. The changes in the quaternary structure caused by this rearrangement are accompanied by a variation of the size of the inner water-filled channel which crosses the PPAT molecule along the threefold axis of the hexamer. The molecular mechanism of the observed changes is described.

PubMed: 23151631
DOI: 10.1107/S0907444912040206

実験手法

X-RAY DIFFRACTION (1.62 Å)