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7JZ2

Succinate: quinone oxidoreductase SQR from E.coli K12

Summary for 7JZ2
Entry DOI10.2210/pdb7jz2/pdb
EMDB information22528
DescriptorSuccinate dehydrogenase flavoprotein subunit, 1,2-Distearoyl-sn-glycerophosphoethanolamine, PROTOPORPHYRIN IX CONTAINING FE, ... (12 entities in total)
Functional Keywordscomplex, succinate: quinone oxidoreductase, sdha, sdhb, sdhc, sdhd, electron transport, electron transport-oxidoreductase complex, electron transport/oxidoreductase
Biological sourceEscherichia coli
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Total number of polymer chains12
Total formula weight365417.91
Authors
Lyu, M.,Su, C.-C.,Morgan, C.E.,Bolla, J.R.,Robinson, C.V.,Yu, E.W. (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 (2.5 Å)
Structure validation

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