2XF1

Crystal structure of Plasmodium falciparum actin depolymerization factor 1

2XF1 の概要

• エントリーDOI: 10.2210/pdb2xf1/pdb
• 分子名称: COFILIN ACTIN-DEPOLYMERIZING FACTOR HOMOLOG 1, SULFATE ION (3 entities in total)
• 機能のキーワード: actin-binding protein, cytoskeleton
• 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: 14568.53

構造登録者

Singh, B.K.,Sattler, J.M.,Huttu, J.,Chatterjee, M.,Schueler, H.,Kursula, I. (登録日: 2010-05-20, 公開日: 2011-06-15, 最終更新日: 2024-11-20)

主引用文献

Singh, B.K.,Sattler, J.M.,Chatterjee, M.,Huttu, J.,Schuler, H.,Kursula, I.
Crystal Structures Explain Functional Differences in the Two Actin Depolymerization Factors of the Malaria Parasite.
J.Biol.Chem., 286:28256-, 2011

PubMed Abstract: Apicomplexan parasites, such as the malaria-causing Plasmodium, utilize an actin-based motor for motility and host cell invasion. The actin filaments of these parasites are unusually short, and actin polymerization is under strict control of a small set of regulatory proteins, which are poorly conserved with their mammalian orthologs. Actin depolymerization factors (ADFs) are among the most important actin regulators, affecting the rates of filament turnover in a multifaceted manner. Plasmodium has two ADFs that display low sequence homology with each other and with the higher eukaryotic family members. Here, we show that ADF2, like canonical ADF proteins but unlike ADF1, binds to both globular and filamentous actin, severing filaments and inducing nucleotide exchange on the actin monomer. The crystal structure of Plasmodium ADF1 shows major differences from the ADF consensus, explaining the lack of F-actin binding. Plasmodium ADF2 structurally resembles the canonical members of the ADF/cofilin family.

PubMed: 21832095
DOI: 10.1074/JBC.M111.211730

実験手法

X-RAY DIFFRACTION (1.96 Å)