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Determination of the Near-Atomic Structure of Non-Purified Oligomeric E. coli Proteins.

ABSTRACT: The roughly purified extract of E. coli proteins has been studied by cryoelectron microscopy, the class-sums containing 2D projections of two proteins (β-galactosidase and 2-oxoglutarate dehydrogenase complex catalytic domain (ODC-CD)), identified in an extract by tandem mass spectrometry, have been distinguished. The structures of these proteins have been solved at near-atomic resolution. De novo simulation of the ODC-CD structure yielded an atomic model that revealed differences in the positions of some amino acid residues of the active center, in comparison with the known crystal structures.

SUBMITTER: Pichkur EB

PROVIDER: S-EPMC8490847 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

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Determination of the Near-Atomic Structure of Non-Purified Oligomeric E. coli Proteins.

Pichkur E B EB Mikirtumov V I VI Tikhonova O V OV Derkacheva N I NI Kurochkina L P LP Sokolova O S OS

Crystallography reports 20211005 5

The roughly purified extract of E. coli proteins has been studied by cryoelectron microscopy, the class-sums containing 2D projections of two proteins (β-galactosidase and 2-oxoglutarate dehydrogenase complex catalytic domain (ODC-CD)), identified in an extract by tandem mass spectrometry, have been distinguished. The structures of these proteins have been solved at near-atomic resolution. De novo simulation of the ODC-CD structure yielded an atomic model that revealed differences ...[more]

PMID: 35173403

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