7MPP
Bartonella henselae NrnC cleaving pGG in the presence of Mg2+
Summary for 7MPP
| Entry DOI | 10.2210/pdb7mpp/pdb |
| Related | 7MPL 7MPM 7MPN 7MPO 7MPQ 7MPR 7MPS 7MPT 7MPU 7MQB 7MQC 7MQD 7MQE 7MQF 7MQG 7MQH 7MQI |
| Descriptor | NanoRNase C, GUANOSINE-5'-MONOPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | rnase, bacteria, enzyme, rna binding protein |
| Biological source | Bartonella henselae (Rochalimaea henselae) |
| Total number of polymer chains | 8 |
| Total formula weight | 193774.22 |
| Authors | Lormand, J.D.,Sondermann, H. (deposition date: 2021-05-04, release date: 2021-09-15, Last modification date: 2023-10-18) |
| Primary citation | Lormand, J.D.,Kim, S.K.,Walters-Marrah, G.A.,Brownfield, B.A.,Fromme, J.C.,Winkler, W.C.,Goodson, J.R.,Lee, V.T.,Sondermann, H. Structural characterization of NrnC identifies unifying features of dinucleotidases. Elife, 10:-, 2021 Cited by PubMed Abstract: RNA degradation is fundamental for cellular homeostasis. The process is carried out by various classes of endolytic and exolytic enzymes that together degrade an RNA polymer to mono-ribonucleotides. Within the exoribonucleases, nano-RNases play a unique role as they act on the smallest breakdown products and hence catalyze the final steps in the process. We recently showed that oligoribonuclease (Orn) acts as a dedicated diribonucleotidase, defining the ultimate step in RNA degradation that is crucial for cellular fitness (Kim et al., 2019). Whether such a specific activity exists in organisms that lack Orn-type exoribonucleases remained unclear. Through quantitative structure-function analyses, we show here that NrnC-type RNases share this narrow substrate length preference with Orn. Although NrnC and Orn employ similar structural features that distinguish these two classes of dinucleotidases from other exonucleases, the key determinants for dinucleotidase activity are realized through distinct structural scaffolds. The structures, together with comparative genomic analyses of the phylogeny of DEDD-type exoribonucleases, indicate convergent evolution as the mechanism of how dinucleotidase activity emerged repeatedly in various organisms. The evolutionary pressure to maintain dinucleotidase activity further underlines the important role these analogous proteins play for cell growth. PubMed: 34533457DOI: 10.7554/eLife.70146 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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