6PEV

CryoEM Plasmodium falciparum M18 aspartyl aminopeptidase

6PEV の概要

• エントリーDOI: 10.2210/pdb6pev/pdb
• EMDBエントリー: 20333
• 分子名称: M18 aspartyl aminopeptidase, ZINC ION (2 entities in total)
• 機能のキーワード: aspartyl aminopeptidase, metal binding protein
• 由来する生物種: Plasmodium falciparum (isolate NF54)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 790232.98

構造登録者

Ho, C.,Lai, M.,Zhou, Z.H. (登録日: 2019-06-21, 公開日: 2019-12-11, 最終更新日: 2024-10-23)

主引用文献

Ho, C.M.,Li, X.,Lai, M.,Terwilliger, T.C.,Beck, J.R.,Wohlschlegel, J.,Goldberg, D.E.,Fitzpatrick, A.W.P.,Zhou, Z.H.
Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu.
Nat.Methods, 17:79-85, 2020

PubMed Abstract: X-ray crystallography often requires non-native constructs involving mutations or truncations, and is challenged by membrane proteins and large multicomponent complexes. We present here a bottom-up endogenous structural proteomics approach whereby near-atomic-resolution cryo electron microscopy (cryoEM) maps are reconstructed ab initio from unidentified protein complexes enriched directly from the endogenous cellular milieu, followed by identification and atomic modeling of the proteins. The proteins in each complex are identified using cryoID, a program we developed to identify proteins in ab initio cryoEM maps. As a proof of principle, we applied this approach to the malaria-causing parasite Plasmodium falciparum, an organism that has resisted conventional structural-biology approaches, to obtain atomic models of multiple protein complexes implicated in intraerythrocytic survival of the parasite. Our approach is broadly applicable for determining structures of undiscovered protein complexes enriched directly from endogenous sources.

PubMed: 31768063
DOI: 10.1038/s41592-019-0637-y

実験手法

ELECTRON MICROSCOPY (3.2 Å)