7AUF

anammox-specific acyl carrier protein from Kuenenia stuttgartiensis; normal refinement

7AUF の概要

• エントリーDOI: 10.2210/pdb7auf/pdb
• 分子名称: Similar to acyl carrier protein, ZINC ION (3 entities in total)
• 機能のキーワード: acyl carrier protein, ladderanes, anammox, fatty acid biosynthesis, lipid binding protein
• 由来する生物種: Kuenenia stuttgartiensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11190.00

構造登録者

Dietl, A.,Barends, T. (登録日: 2020-11-03, 公開日: 2021-08-11, 最終更新日: 2024-06-19)

主引用文献

Dietl, A.,Barends, T.R.M.
Dynamics in an unusual acyl carrier protein from a ladderane lipid-synthesizing organism.
Proteins, 90:73-82, 2022

PubMed Abstract: Anaerobic ammonium-oxidizing (anammox) bacteria express a distinct acyl carrier protein implicated in the biosynthesis of the highly unusual "ladderane" lipids these organisms produce. This "anammox-specific" ACP, or amxACP, shows several unique features such as a conserved FF motif and an unusual sequence in the functionally important helix III. Investigation of the protein's structure and dynamics, both in the crystal by ensemble refinement and by MD simulations, reveals that helix III adopts a rare six-residue-long 3 -helical conformation that confers a large degree of conformational and positional variability on this part of the protein. This way of introducing structural flexibility by using the inherent properties of 3 -helices appears unique among ACPs. Moreover, the structure suggests a role for the FF motif in shielding the thioester linkage between the protein's prosthetic group and its acyl cargo from hydrolysis.

PubMed: 34310758
DOI: 10.1002/prot.26187

実験手法

X-RAY DIFFRACTION (1.76 Å)