7EVK
Odinarchaeota tubulin (OdinTubulin) H393D mutant, in a protofilament arrangement, bound to 78% GTP, 22% GDP, Na+
Summary for 7EVK
| Entry DOI | 10.2210/pdb7evk/pdb |
| Descriptor | Tubulin-like protein, GUANOSINE-5'-TRIPHOSPHATE, GUANOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | asgard, tubulin, gtp, filament, structural protein |
| Biological source | Odinarchaeota archaeon (strain LCB_4) |
| Total number of polymer chains | 1 |
| Total formula weight | 48645.77 |
| Authors | Robinson, R.C.,Akil, C.,Tran, L.T. (deposition date: 2021-05-21, release date: 2022-03-23, Last modification date: 2023-11-29) |
| Primary citation | Akil, C.,Ali, S.,Tran, L.T.,Gaillard, J.,Li, W.,Hayashida, K.,Hirose, M.,Kato, T.,Oshima, A.,Fujishima, K.,Blanchoin, L.,Narita, A.,Robinson, R.C. Structure and dynamics of Odinarchaeota tubulin and the implications for eukaryotic microtubule evolution. Sci Adv, 8:eabm2225-eabm2225, 2022 Cited by PubMed Abstract: Tubulins are critical for the internal organization of eukaryotic cells, and understanding their emergence is an important question in eukaryogenesis. Asgard archaea are the closest known prokaryotic relatives to eukaryotes. Here, we elucidated the apo and nucleotide-bound x-ray structures of an Asgard tubulin from hydrothermal living Odinarchaeota (OdinTubulin). The guanosine 5'-triphosphate (GTP)-bound structure resembles a microtubule protofilament, with GTP bound between subunits, coordinating the "+" end subunit through a network of water molecules and unexpectedly by two cations. A water molecule is located suitable for GTP hydrolysis. Time course crystallography and electron microscopy revealed conformational changes on GTP hydrolysis. OdinTubulin forms tubules at high temperatures, with short curved protofilaments coiling around the tubule circumference, more similar to FtsZ, rather than running parallel to its length, as in microtubules. Thus, OdinTubulin represents an evolutionary stage intermediate between prokaryotic FtsZ and eukaryotic microtubule-forming tubulins. PubMed: 35333570DOI: 10.1126/sciadv.abm2225 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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