6RK6
Characterization of an intertidal zone metagenome oligoribonuclease and the role of the intermolecular disulfide bond for homodimer formation and nuclease activity.
Summary for 6RK6
| Entry DOI | 10.2210/pdb6rk6/pdb |
| Descriptor | Oligoribonuclease, MANGANESE (II) ION (2 entities in total) |
| Functional Keywords | oligoribonuclease, metagenome, rna, homodimer, hydrolase |
| Biological source | metagenome |
| Total number of polymer chains | 3 |
| Total formula weight | 64819.51 |
| Authors | Piotrowski, Y.,Berg, K.,Klebl, D.P.,Leiros, I.,Larsen, A.N. (deposition date: 2019-04-30, release date: 2019-08-28, Last modification date: 2024-11-06) |
| Primary citation | Piotrowski, Y.,Berg, K.,Klebl, D.P.,Leiros, I.,Larsen, A.N. Characterization of an intertidal zone metagenome oligoribonuclease and the role of the intermolecular disulfide bond for homodimer formation and nuclease activity. Febs Open Bio, 9:1674-1688, 2019 Cited by PubMed Abstract: The gene encoding MG Orn has been identified from a metagenomic library created from the intertidal zone in Svalbard and encodes a protein of 184 amino acid residues. The mg orn gene has been cloned, recombinantly expressed in Escherichia coli, and purified to homogeneity. Biochemical characterization of the enzyme showed that it efficiently degrades short RNA oligonucleotide substrates of 2mer to 10mer of length and has an absolute requirement for divalent cations for optimal activity. The enzyme is more heat-labile than its counterpart from E. coli and exists as a homodimer in solution. The crystal structure of the enzyme has been determined to a resolution of 3.15 Å, indicating an important role of a disulfide bridge for the homodimer formation and as such for the function of MG Orn. Substitution of the Cys110 residue with either Gly or Ala hampered the dimer formation and severely affected the enzyme's ability to act on RNA. A conserved loop containing His128-Tyr129-Arg130 in the neighboring monomer is probably involved in efficient binding and processing of longer RNA substrates than diribonucleotides. PubMed: 31420950DOI: 10.1002/2211-5463.12720 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
Download full validation report
