3DCO
Drosophila NOD (3DC4) and Bovine Tubulin (1JFF) Docked into the 11-Angstrom Cryo-EM Map of Nucleotide-Free NOD Complexed to the Microtubule
Summary for 3DCO
| Entry DOI | 10.2210/pdb3dco/pdb |
| Related | 1JFF 3DC4 3DCB |
| EMDB information | 5038 |
| Descriptor | Kinesin-like protein Nod, Bovine Alpha Tubulin, Bovine Beta Tubulin, ... (9 entities in total) |
| Functional Keywords | kinesin, catalytic domain, atpase, microtubule, adp, nucleotide-binding protein, cryo-em, 3d reconstruction, tubulin, nucleotide-free, atp-binding, coiled coil, motor protein, nucleotide-binding |
| Biological source | Drosophila melanogaster (Fruit fly) More |
| Total number of polymer chains | 3 |
| Total formula weight | 140682.08 |
| Authors | Sindelar, C.V.,Cochran, J.C.,Kull, F.J. (deposition date: 2008-06-04, release date: 2009-02-10, Last modification date: 2024-02-21) |
| Primary citation | Cochran, J.C.,Sindelar, C.V.,Mulko, N.K.,Collins, K.A.,Kong, S.E.,Hawley, R.S.,Kull, F.J. ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement. Cell(Cambridge,Mass.), 136:110-122, 2009 Cited by PubMed Abstract: Segregation of nonexchange chromosomes during Drosophila melanogaster meiosis requires the proper function of NOD, a nonmotile kinesin-10. We have determined the X-ray crystal structure of the NOD catalytic domain in the ADP- and AMPPNP-bound states. These structures reveal an alternate conformation of the microtubule binding region as well as a nucleotide-sensitive relay of hydrogen bonds at the active site. Additionally, a cryo-electron microscopy reconstruction of the nucleotide-free microtubule-NOD complex shows an atypical binding orientation. Thermodynamic studies show that NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including AMPPNP, are weakened. Our pre-steady-state kinetic analysis demonstrates that NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis, which is also atypical for a kinesin. We propose a model for NOD's microtubule plus-end tracking that drives chromosome movement. PubMed: 19135893DOI: 10.1016/j.cell.2008.11.048 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (11 Å) |
Structure validation
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