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5LXR

Structure of the minimal RBM7 - ZCCHC8 Complex

Summary for 5LXR
Entry DOI10.2210/pdb5lxr/pdb
DescriptorRNA-binding protein 7, Zinc finger CCHC domain-containing protein 8, SAMARIUM (III) ION, ... (6 entities in total)
Functional Keywordsnext complex rrm rbm7 zcchc8, rna binding protein
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus, nucleoplasm : Q6NZY4
Total number of polymer chains2
Total formula weight15936.72
Authors
Falk, S.,Finogenova, K.,Benda, C.,Conti, E. (deposition date: 2016-09-22, release date: 2016-12-14, Last modification date: 2024-05-08)
Primary citationFalk, S.,Finogenova, K.,Melko, M.,Benda, C.,Lykke-Andersen, S.,Jensen, T.H.,Conti, E.
Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors.
Nat Commun, 7:13573-13573, 2016
Cited by
PubMed Abstract: The eukaryotic RNA exosome participates extensively in RNA processing and degradation. In human cells, three accessory factors (RBM7, ZCCHC8 and hMTR4) interact to form the nuclear exosome targeting (NEXT) complex, which directs a subset of non-coding RNAs for exosomal degradation. Here we elucidate how RBM7 is incorporated in the NEXT complex. We identify a proline-rich segment of ZCCHC8 as the interaction site for the RNA-recognition motif (RRM) of RBM7 and present the crystal structure of the corresponding complex at 2.0 Å resolution. On the basis of the structure, we identify a proline-rich segment within the splicing factor SAP145 with strong similarity to ZCCHC8. We show that this segment of SAP145 not only binds the RRM region of another splicing factor SAP49 but also the RRM of RBM7. These dual interactions of RBM7 with the exosome and the spliceosome suggest a model whereby NEXT might recruit the exosome to degrade intronic RNAs.
PubMed: 27905398
DOI: 10.1038/ncomms13573
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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