6PEV

CryoEM Plasmodium falciparum M18 aspartyl aminopeptidase

Summary for 6PEV

• Entry DOI: 10.2210/pdb6pev/pdb
• EMDB information: 20333
• Descriptor: M18 aspartyl aminopeptidase, ZINC ION (2 entities in total)
• Functional Keywords: aspartyl aminopeptidase, metal binding protein
• Biological source: Plasmodium falciparum (isolate NF54)
• Total number of polymer chains: 12
• Total formula weight: 790232.98

Authors

Ho, C.,Lai, M.,Zhou, Z.H. (deposition date: 2019-06-21, release date: 2019-12-11, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.2 Å)