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8VES

Structure of YicC endoribonuclease bound to an RNA substrate

Summary for 8VES
Entry DOI10.2210/pdb8ves/pdb
EMDB information43173
DescriptorEndoribonuclease YicC, RNA (26-MER) (3 entities in total)
Functional Keywordsendoribonuclease, hexamer, e. coli, hydrolase
Biological sourceEscherichia coli
More
Total number of polymer chains7
Total formula weight208667.39
Authors
Wu, R.,Lazarus, M.B. (deposition date: 2023-12-20, release date: 2024-09-04, Last modification date: 2024-10-09)
Primary citationWu, R.,Ingle, S.,Barnes, S.A.,Dahlin, H.R.,Khamrui, S.,Xiang, Y.,Shi, Y.,Bechhofer, D.H.,Lazarus, M.B.
Structural insights into RNA cleavage by a novel family of bacterial RNases.
Nucleic Acids Res., 52:10705-10716, 2024
Cited by
PubMed Abstract: Processing of RNA is a key regulatory mechanism for all living systems. Escherichia coli protein YicC belongs to the well-conserved YicC family and has been identified as a novel ribonuclease. Here, we report a 2.8-Å-resolution crystal structure of the E. coli YicC apo protein and a 3.2-Å-cryo-EM structure of YicC bound to an RNA substrate. The apo YicC forms a dimer of trimers with a large open channel. In the RNA-bound form, the top trimer of YicC rotates nearly 70° and closes the RNA substrate inside the cavity to form a clamshell-pearl conformation that resembles no other known RNases. The structural information combined with mass spectrometry and biochemical data identified cleavage on the upstream side of an RNA hairpin. Mutagenesis studies demonstrated that the previously uncharacterized domain, DUF1732, is critical in both RNA binding and catalysis. These studies shed light on the mechanism of the previously unexplored YicC RNase family.
PubMed: 39180400
DOI: 10.1093/nar/gkae717
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.22 Å)
Structure validation

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PDB entries from 2024-11-20

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