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2JEA

Structure of a 9-subunit archaeal exosome bound to RNA

Summary for 2JEA
Entry DOI10.2210/pdb2jea/pdb
Related2BR2 2C37 2C38 2C39 2JE6 2JEB
DescriptorEXOSOME COMPLEX EXONUCLEASE 2, EXOSOME COMPLEX EXONUCLEASE 1, RNA, ... (6 entities in total)
Functional Keywordshydrolase rna complex, hydrolase-rna complex, nuclease, hydrolase, rna-binding, exonuclease, phosphorolytic, exoribonuclease, rna degradation, rrp4, rrp42, rrp41, exosome, rnase ph, hydrolase/rna
Biological sourceSULFOLOBUS SOLFATARICUS
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Cellular locationCytoplasm (Potential): Q9UXC0 2JEA Q9UXC2
Total number of polymer chains4
Total formula weight98079.60
Authors
Lorentzen, E.,Conti, E. (deposition date: 2007-01-16, release date: 2007-04-03, Last modification date: 2023-12-13)
Primary citationLorentzen, E.,Dziembowski, A.,Lindner, D.,Seraphin, B.,Conti, E.
RNA Channelling by the Archaeal Exosome.
Embo Rep., 8:470-, 2007
Cited by
PubMed Abstract: Exosomes are complexes containing 3' --> 5' exoribonucleases that have important roles in processing, decay and quality control of various RNA molecules. Archaeal exosomes consist of a hexameric core of three active RNase PH subunits (ribosomal RNA processing factor (Rrp)41) and three inactive RNase PH subunits (Rrp42). A trimeric ring of subunits with putative RNA-binding domains (Rrp4/cep1 synthetic lethality (Csl)4) is positioned on top of the hexamer on the opposite side to the RNA degrading sites. Here, we present the 1.6 A resolution crystal structure of the nine-subunit exosome of Sulfolobus solfataricus and the 2.3 A structure of this complex bound to an RNA substrate designed to be partly trimmed rather than completely degraded. The RNA binds both at the active site on one side of the molecule and on the opposite side in the narrowest constriction of the central channel. Multiple substrate-binding sites and the entrapment of the substrate in the central channel provide a rationale for the processive degradation of extended RNAs and the stalling of structured RNAs.
PubMed: 17380186
DOI: 10.1038/SJ.EMBOR.7400945
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.33 Å)
Structure validation

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数据于2025-07-09公开中

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