5ZWT

Crystal structure of the S37A mutant of apo-acyl carrier protein from Leishmania major

5ZWT の概要

• エントリーDOI: 10.2210/pdb5zwt/pdb
• 関連するPDBエントリー: 2M5R
• 分子名称: Acyl carrier protein (2 entities in total)
• 機能のキーワード: leishmania major; acyl carrier protein; fatty acid biosynthesis, lipid binding protein
• 由来する生物種: Leishmania major
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18542.97

構造登録者

Sharma, B.,Arya, R.,Kundu, S.,Makde, R.D. (登録日: 2018-05-16, 公開日: 2019-01-16, 最終更新日: 2023-11-22)

主引用文献

Arya, R.,Sharma, B.,Dhembla, C.,Pal, R.K.,Patel, A.K.,Sundd, M.,Ghosh, B.,Makde, R.D.,Kundu, S.
A conformational switch from a closed apo- to an open holo-form equips the acyl carrier protein for acyl chain accommodation.
Biochim Biophys Acta Proteins Proteom, 1867:163-174, 2018

PubMed Abstract: Acyl carrier proteins (ACPs) play crucial roles in the biosynthesis of fatty acids, non-ribosomal polypeptides and polyketides. The three-dimensional NMR structure of Leishmania major holo-LmACP, belonging to the type II pathway, has been reported previously, but the structure of its apo-form and its conformational differences with the holo-form remain to be explored. Here we report the crystal structures of apo-LmACP (wild-type and S37A mutant) at 2.0 Å resolution and compare their key features with the structures of holo-LmACP (wild-type) and other type II ACPs from Escherichia coli and Plasmodium falciparum. The crystal structure of apo-LmACP, which is homologous to other type II ACPs, displays some key structural rearrangements as compared to its holo-structure. Contrary to holo-form, which exists predominantly as a monomer, the apo-form exists as a mixture of monomeric and dimeric population in solution. In contrast to the closed structure of apo-LmACP, holo-LmACP structure was observed in an open conformation as a result of reorganization of specific helices and loops. We propose that the structural changes exhibited by LmACP occur due to the attachment of the phosphopantetheine arm and may be a prerequisite for the initiation of fatty acid synthesis. The movement of helix 3 may also play a role in the dissociation of holo-LmACP from its cognate enzymes of the FAS II pathway.

PubMed: 30543875
DOI: 10.1016/j.bbapap.2018.12.001

実験手法

X-RAY DIFFRACTION (2 Å)