5YU2
Structure of Ribonuclease YabJ
Summary for 5YU2
| Entry DOI | 10.2210/pdb5yu2/pdb |
| Descriptor | Translation initiation inhibitor homologue (2 entities in total) |
| Functional Keywords | sav0497, yabj, ribonuclease, gene regulation |
| Biological source | Staphylococcus aureus (strain Mu50 / ATCC 700699) |
| Total number of polymer chains | 6 |
| Total formula weight | 85658.31 |
| Authors | Kim, H.J.,Kwon, A.R.,Lee, B.J. (deposition date: 2017-11-20, release date: 2018-09-26, Last modification date: 2023-11-22) |
| Primary citation | Kim, H.J.,Kwon, A.R.,Lee, B.J. A novel chlorination-induced ribonuclease YabJ fromStaphylococcus aureus. Biosci. Rep., 38:-, 2018 Cited by PubMed Abstract: The characteristic fold of a protein is the decisive factor for its biological function. However, small structural changes to amino acids can also affect their function, for example in the case of post-translational modification (PTM). Many different types of PTMs are known, but for some, including chlorination, studies elucidating their importance are limited. A recent study revealed that the YjgF/YER057c/UK114 family (YjgF family) member RidA from shows chaperone activity after chlorination. Thus, to identify the functional and structural differences of RidA upon chlorination, we studied an RidA homolog from : YabJ. The overall structure of YabJ was similar to other members of the YjgF family, showing deep pockets on its surface, and the residues composing the pockets were well conserved. YabJ was highly stable after chlorination, and the chlorinated state is reversible by treatment with DTT. However, it shows no chaperone activity after chlorination. Instead, YabJ from shows chlorination-induced ribonuclease activity, and the activity is diminished after subsequent reduction. Even though the genes from and are clustered with regulators that are expected to code nucleic acid-interacting proteins, the nucleic acid-related activity of bacterial RidA has not been identified before. From our study, we revealed the structure and function of YabJ as a novel chlorination-activated ribonuclease. The present study will contribute to an in-depth understanding of chlorination as a PTM. PubMed: 30201692DOI: 10.1042/BSR20180768 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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