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5KL8

Crystal structure of the Pumilio-Nos-CyclinB RNA complex

Summary for 5KL8
Entry DOI10.2210/pdb5kl8/pdb
Related5KL1 5KLA
DescriptorMaternal protein pumilio, Protein nanos, RNA (5'-R(*UP*AP*UP*UP*UP*GP*UP*AP*AP*UP*U)-3'), ... (4 entities in total)
Functional Keywordsrna-binding proteins, rna-binding protein-rna complex, rna-binding protein/rna
Biological sourceDrosophila melanogaster (Fruit fly)
More
Cellular locationCytoplasm : P25822
Total number of polymer chains3
Total formula weight56289.61
Authors
Qiu, C.,Hall, T.M.T. (deposition date: 2016-06-23, release date: 2016-08-17, Last modification date: 2024-03-06)
Primary citationWeidmann, C.A.,Qiu, C.,Arvola, R.M.,Lou, T.F.,Killingsworth, J.,Campbell, Z.T.,Tanaka Hall, T.M.,Goldstrohm, A.C.
Drosophila Nanos acts as a molecular clamp that modulates the RNA-binding and repression activities of Pumilio.
Elife, 5:-, 2016
Cited by
PubMed Abstract: Collaboration among the multitude of RNA-binding proteins (RBPs) is ubiquitous, yet our understanding of these key regulatory complexes has been limited to single RBPs. We investigated combinatorial translational regulation by Drosophila Pumilio (Pum) and Nanos (Nos), which control development, fertility, and neuronal functions. Our results show how the specificity of one RBP (Pum) is modulated by cooperative RNA recognition with a second RBP (Nos) to synergistically repress mRNAs. Crystal structures of Nos-Pum-RNA complexes reveal that Nos embraces Pum and RNA, contributes sequence-specific contacts, and increases Pum RNA-binding affinity. Nos shifts the recognition sequence and promotes repression complex formation on mRNAs that are not stably bound by Pum alone, explaining the preponderance of sub-optimal Pum sites regulated in vivo. Our results illuminate the molecular mechanism of a regulatory switch controlling crucial gene expression programs, and provide a framework for understanding how the partnering of RBPs evokes changes in binding specificity that underlie regulatory network dynamics.
PubMed: 27482653
DOI: 10.7554/eLife.17096
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4 Å)
Structure validation

226707

数据于2024-10-30公开中

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