Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7JZ6

The Cryo-EM structure of the Catalase-peroxidase from Escherichia coli

Summary for 7JZ6
Entry DOI10.2210/pdb7jz6/pdb
EMDB information22530
DescriptorCatalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordscatalase-peroxidase, oxidoreductase
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight322916.29
Authors
Su, C.-C. (deposition date: 2020-09-01, release date: 2021-01-20, Last modification date: 2024-03-06)
Primary citationSu, C.C.,Lyu, M.,Morgan, C.E.,Bolla, J.R.,Robinson, C.V.,Yu, E.W.
A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins.
Nat.Methods, 18:69-75, 2021
Cited by
PubMed Abstract: Single-particle cryo-electron microscopy (cryo-EM) has become a powerful technique in the field of structural biology. However, the inability to reliably produce pure, homogeneous membrane protein samples hampers the progress of their structural determination. Here, we develop a bottom-up iterative method, Build and Retrieve (BaR), that enables the identification and determination of cryo-EM structures of a variety of inner and outer membrane proteins, including membrane protein complexes of different sizes and dimensions, from a heterogeneous, impure protein sample. We also use the BaR methodology to elucidate structural information from Escherichia coli K12 crude membrane and raw lysate. The findings demonstrate that it is possible to solve high-resolution structures of a number of relatively small (<100 kDa) and less abundant (<10%) unidentified membrane proteins within a single, heterogeneous sample. Importantly, these results highlight the potential of cryo-EM for systems structural proteomics.
PubMed: 33408407
DOI: 10.1038/s41592-020-01021-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.53 Å)
Structure validation

226707

数据于2024-10-30公开中

PDB statisticsPDBj update infoContact PDBjnumon