4M2Z
Crystal structure of RNASE III complexed with double-stranded RNA and CMP (TYPE II CLEAVAGE)
Summary for 4M2Z
| Entry DOI | 10.2210/pdb4m2z/pdb |
| Related | 2NUG 4M30 |
| Descriptor | Ribonuclease 3, RNA10, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | rnase iii, hydrolase, dsrna, rna binding, rna processing, hydrolase-rna complex, hydrolase/rna |
| Biological source | Aquifex aeolicus More |
| Cellular location | Cytoplasm (By similarity): O67082 |
| Total number of polymer chains | 4 |
| Total formula weight | 70497.42 |
| Authors | Gan, J.,Liang, Y.-H.,Shaw, G.X.,Tropea, J.E.,Waugh, D.S.,Ji, X. (deposition date: 2013-08-05, release date: 2013-12-11, Last modification date: 2024-07-03) |
| Primary citation | Court, D.L.,Gan, J.,Liang, Y.H.,Shaw, G.X.,Tropea, J.E.,Costantino, N.,Waugh, D.S.,Ji, X. RNase III: Genetics and Function; Structure and Mechanism. Annu. Rev. Genet., 47:405-431, 2013 Cited by PubMed Abstract: RNase III is a global regulator of gene expression in Escherichia coli that is instrumental in the maturation of ribosomal and other structural RNAs. We examine here how RNase III itself is regulated in response to growth and other environmental changes encountered by the cell and how, by binding or processing double-stranded RNA (dsRNA) intermediates, RNase III controls the expression of genes. Recent insight into the mechanism of dsRNA binding and processing, gained from structural studies of RNase III, is reviewed. Structural studies also reveal new cleavage sites in the enzyme that can generate longer 3' overhangs. PubMed: 24274754DOI: 10.1146/annurev-genet-110711-155618 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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