Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6N6K

Human REXO2 bound to pAG

Summary for 6N6K
Entry DOI10.2210/pdb6n6k/pdb
DescriptorRNA exonuclease 2 homolog,Small fragment nuclease, RNA (5'-R(P*AP*G)-3'), MALONATE ION, ... (5 entities in total)
Functional Keywords3'-5' exoribonuclease, rna binding protein, rna binding protein-rna complex, rna binding protein/rna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight48985.51
Authors
Lormand, J.D.,Sondermann, H. (deposition date: 2018-11-26, release date: 2019-06-12, Last modification date: 2023-10-11)
Primary citationKim, S.K.,Lormand, J.D.,Weiss, C.A.,Eger, K.A.,Turdiev, H.,Turdiev, A.,Winkler, W.C.,Sondermann, H.,Lee, V.T.
A dedicated diribonucleotidase resolves a key bottleneck for the terminal step of RNA degradation.
Elife, 8:-, 2019
Cited by
PubMed Abstract: Degradation of RNA polymers, an ubiquitous process in all cells, is catalyzed by specific subsets of endo- and exoribonucleases that together recycle RNA fragments into nucleotide monophosphate. In γ-proteobacteria, 3-'5' exoribonucleases comprise up to eight distinct enzymes. Among them, Oligoribonuclease (Orn) is unique as its activity is required for clearing short RNA fragments, which is important for cellular fitness. However, the molecular basis of Orn's unique cellular function remained unclear. Here, we show that Orn exhibits exquisite substrate preference for diribonucleotides. Crystal structures of substrate-bound Orn reveal an active site optimized for diribonucleotides. While other cellular RNases process oligoribonucleotides down to diribonucleotide entities, Orn is the one and only diribonucleotidase that completes the terminal step of RNA degradation. Together, our studies indicate RNA degradation as a step-wise process with a dedicated enzyme for the clearance of a specific intermediate pool, diribonucleotides, that affects cellular physiology and viability.
PubMed: 31225796
DOI: 10.7554/eLife.46313
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.418 Å)
Structure validation

229183

PDB entries from 2024-12-18

PDB statisticsPDBj update infoContact PDBjnumon