Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6N6I

Human REXO2 bound to pGG

Summary for 6N6I
Entry DOI10.2210/pdb6n6i/pdb
DescriptorRNA exonuclease 2 homolog,Small fragment nuclease, RNA (5'-R(P*GP*G)-3'), GLYCEROL, ... (7 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 weight49263.77
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 (1.431 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon