2FQ0

Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum

2FQ0 の概要

• エントリーDOI: 10.2210/pdb2fq0/pdb
• 関連するPDBエントリー: 2BAR 2FQ3
• NMR情報: BMRB: 6516
• 分子名称: acyl carrier protein, 4'-PHOSPHOPANTETHEINE (2 entities in total)
• 機能のキーワード: holo-pfacp, 4'-phosphopantetheine, lipid transport
• 由来する生物種: Plasmodium falciparum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9374.52

構造登録者

Sharma, A.K.,Sharma, S.K.,Surolia, A.,Surolia, N.,Sarma, S.P. (登録日: 2006-01-17, 公開日: 2006-08-08, 最終更新日: 2025-03-26)

主引用文献

Sharma, A.K.,Sharma, S.K.,Surolia, A.,Surolia, N.,Sarma, S.P.
Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs
Biochemistry, 45:6904-6916, 2006

PubMed Abstract: Acyl Carrier Protein (ACP) from the malaria parasite, Plasmodium falciparum (PfACP) in its holo form is found to exist in two conformational states in solution. Unique 3D solution structures of holo-PfACP have been determined for both equilibrium conformations, using high-resolution NMR methods. Twenty high-resolution solution structures for each of the two forms of holo-PfACP have been determined on the basis of 1226 and 1218 unambiguously assigned NOEs (including NOEs between 4'-phosphopantetheine prosthetic group (4'-PP) and protein), 55 backbone dihedral angles and 26 hydrogen bonds. The atomic rmsd values of the determined structures of two equilibrium forms, about the mean coordinates of the backbone and heavy atoms, are 0.48 +/- 0.09 and 0.92 +/- 0.10 and 0.49 +/- 0.08 and 0.97 +/- 0.11 A, respectively. The interaction of 4'-PP with the polypeptide backbone is reported here for the first time for any of the ACPs. The structures of holo-PfACP consist of three well-defined helices that are tightly packed. The structured regions of the molecule are stabilized by extensive hydrophobic interactions. The difference between the two forms arises from a reorientation of the 4'-PP group. The enthalpy difference between the two forms, although small, implies that a conformational switch is essential for the activation of holo-ACP. Sequence and structures of holo-PfACP have been compared with those of the ACPs from type I and type II fatty acid biosynthesis pathways (FAS), in particular with the ACP from rat and the butyryl-ACP from E. coli. The PfACP structure, thus determined has several novel features hitherto not seen in other ACPs.

PubMed: 16734426
DOI: 10.1021/bi060368u

実験手法

SOLUTION NMR