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6H3Z

Crystal structure of a C-terminal MIF4G domain in NOT1

Summary for 6H3Z
Entry DOI10.2210/pdb6h3z/pdb
DescriptorCCR4-not transcription complex subunit 1, SODIUM ION (2 entities in total)
Functional Keywordsgene regulation, deadenylation, mrna decay, ccr4-not, hydrolase, transcription
Biological sourceChaetomium thermophilum var. thermophilum DSM 1495
Total number of polymer chains2
Total formula weight50790.20
Authors
Raisch, T.,Sandmeir, F.,Weichenrieder, O.,Valkov, E.,Izaurralde, E. (deposition date: 2018-07-19, release date: 2018-11-07, Last modification date: 2024-05-15)
Primary citationRaisch, T.,Sandmeir, F.,Weichenrieder, O.,Valkov, E.,Izaurralde, E.
Structural and biochemical analysis of a NOT1 MIF4G-like domain of the CCR4-NOT complex.
J. Struct. Biol., 204:388-395, 2018
Cited by
PubMed Abstract: The CCR4-NOT complex plays a central role in the regulation of gene expression and degradation of messenger RNAs. The multisubunit complex assembles on the NOT1 protein, which acts as a 'scaffold' and is highly conserved in eukaryotes. NOT1 consists of a series of helical domains that serve as docking sites for other CCR4-NOT subunits. We describe a crystal structure of a connector domain of NOT1 from the thermophilic fungus Chaetomium thermophilum (Ct). Comparative structural analysis indicates that this domain adopts a MIF4G-like fold and we have termed it the MIF4G-C domain. Solution scattering studies indicate that the human MIF4G-C domain likely adopts a very similar fold to the Ct MIF4G-C. MIF4G domains have been described to mediate interactions with DEAD-box helicases such as DDX6. However, comparison of the interfaces of the MIF4G-C with the MIF4G domain of NOT1 that interacts with DDX6 reveals key structural differences that explain why the MIF4G-C does not bind DDX6. We further show that the human MIF4G-C does not interact stably with other subunits of the CCR4-NOT complex. The structural conservation of the MIF4G-C domain suggests that it may have an important but presently undefined role in the CCR4-NOT complex.
PubMed: 30367941
DOI: 10.1016/j.jsb.2018.10.009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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