Structural highlights
Function[ECX2_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). [ECR1_SULSO] Probably involved in degradation of a variety of RNA species; could act a RNA-binding component of the exosome (Potential). [ECX1_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: The exosome complex is an essential RNA 3'-end processing and degradation machinery. In archaeal organisms, the exosome consists of a catalytic ring and an RNA-binding ring, both of which were previously reported to assume three-fold symmetry. METHODOLOGY/PRINCIPAL FINDINGS: Here we report an asymmetric 2.9 A Sulfolobus solfataricus archaeal exosome structure in which the three-fold symmetry is broken due to combined rigid body and thermal motions mainly within the RNA-binding ring. Since increased conformational flexibility was also observed in the RNA-binding ring of the related bacterial PNPase, we speculate that this may reflect an evolutionarily conserved mechanism to accommodate diverse RNA substrates for degradation. CONCLUSION/SIGNIFICANCE: This study clearly shows the dynamic structures within the RNA-binding domains, which provides additional insights on mechanism of asymmetric RNA binding and processing. Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring.,Lu C, Ding F, Ke A PLoS One. 2010 Jan 15;5(1):e8739. PMID:20090900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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