5IQQ

Crystal structure of the human RBM7 RRM domain

Summary for 5IQQ

• Entry DOI: 10.2210/pdb5iqq/pdb
• Descriptor: RNA-binding protein 7 (2 entities in total)
• Functional Keywords: pentameric assembly, rrm fold, non-crystallographic symmetry, rna binding protein, next complex, exosome, rna degradation
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 5
• Total formula weight: 50583.79

Authors

Sofos, N.,Winkler, M.B.L.,Brodersen, D.E. (deposition date: 2016-03-11, release date: 2016-05-04, Last modification date: 2024-01-10)

Primary citation

Sofos, N.,Winkler, M.B.,Brodersen, D.E.
RRM domain of human RBM7: purification, crystallization and structure determination.
Acta Crystallogr.,Sect.F, 72:397-402, 2016

PubMed Abstract: RNA decay is an important process that is essential for controlling the abundance, quality and maturation of transcripts. In eukaryotes, RNA decay in the 3'-5' direction is carried out by the exosome, an RNA-degradation machine that is conserved from yeast to humans. A range of cofactors stimulate the enzymatic activity of the exosome and serve as adapters for the many RNA substrates. In human cells, the exosome associates with the heterotrimeric nuclear exosome targeting (NEXT) complex consisting of the DExH-box helicase hMTR4, the zinc-finger protein hZCCHC8 and the RRM-type protein hRBM7. Here, the 2.5 Å resolution crystal structure of the RRM domain of human RBM7 is reported. Molecular replacement using a previously determined solution structure of RBM7 was unsuccessful. Instead, RBM8 and CBP20 RRM-domain crystal structures were used to successfully determine the RBM7 structure by molecular replacement. The structure reveals a ring-shaped pentameric assembly, which is most likely a consequence of crystal packing.

PubMed: 27139832
DOI: 10.1107/S2053230X16006129

Experimental method

X-RAY DIFFRACTION (2.52 Å)