7MDI
Structure of the Neisseria gonorrhoeae ribonucleotide reductase in the inactive state
Summary for 7MDI
| Entry DOI | 10.2210/pdb7mdi/pdb |
| EMDB information | 23773 |
| Descriptor | Ribonucleoside-diphosphate reductase subunit alpha, Ribonucleoside-diphosphate reductase subunit beta, CYTIDINE-5'-DIPHOSPHATE, ... (7 entities in total) |
| Functional Keywords | inactive complex, ribonucleotide reductase, oxidoreductase |
| Biological source | Neisseria gonorrhoeae More |
| Total number of polymer chains | 8 |
| Total formula weight | 535003.87 |
| Authors | Levitz, T.S.,Drennan, C.L.,Brignole, E.J. (deposition date: 2021-04-05, release date: 2022-01-05, Last modification date: 2024-05-29) |
| Primary citation | Levitz, T.S.,Brignole, E.J.,Fong, I.,Darrow, M.C.,Drennan, C.L. Effects of chameleon dispense-to-plunge speed on particle concentration, complex formation, and final resolution: A case study using the Neisseria gonorrhoeae ribonucleotide reductase inactive complex. J.Struct.Biol., 214:107825-107825, 2021 Cited by PubMed Abstract: Ribonucleotide reductase (RNR) is an essential enzyme that converts ribonucleotides to deoxyribonucleotides and is a promising antibiotic target, but few RNRs have been structurally characterized. We present the use of the chameleon, a commercially-available piezoelectric cryogenic electron microscopy plunger, to address complex denaturation in the Neisseria gonorrhoeae class Ia RNR. Here, we characterize the extent of denaturation of the ring-shaped complex following grid preparation using a traditional plunger and using a chameleon with varying dispense-to-plunge times. We also characterize how dispense-to-plunge time influences the amount of protein sample required for grid preparation and preferred orientation of the sample. We demonstrate that the fastest dispense-to-plunge time of 54 ms is sufficient for generation of a data set that produces a high quality structure, and that a traditional plunging technique or slow chameleon dispense-to-plunge times generate data sets limited in resolution by complex denaturation. The 4.3 Å resolution structure of Neisseria gonorrhoeae class Ia RNR in the inactive α4β4 oligomeric state solved using the chameleon with a fast dispense-to-plunge time yields molecular information regarding similarities and differences to the well studied Escherichia coli class Ia RNR α4β4 ring. PubMed: 34906669DOI: 10.1016/j.jsb.2021.107825 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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