4F61: Tubulin:stathmin-Like Domain Complex

Citation:
Abstract
In cells, microtubule dynamics is regulated by stabilizing and destabilizing factors. Whereas proteins in both categories have been identified, their mechanism of action is rarely understood at the molecular level. This is due in part to the difficulties faced in structural approaches to obtain atomic models when tubulin is involved. Here, we design and characterize new stathmin-like domain (SLD) proteins that sequester tubulins in numbers different from two, the number of tubulins bound by stathmin or by the SLD of RB3, two stathmin family members that have been extensively studied. We established rules for the design of tight tubulin-SLD assemblies and applied them to complexes containing one to four tubulin heterodimers. Biochemical and structural experiments showed that the engineered SLDs behaved as expected. The new SLDs will be tools for structural studies of microtubule regulation. The larger complexes will be useful for cryo-electron microscopy, whereas crystallography or nuclear magnetic resonance will benefit from the 1:1 tubulin-SLD assembly. Finally, our results provide new insight into SLD function, suggesting that a major effect of these phosphorylatable proteins is the programmed release of sequestered tubulin for microtubule assembly at the specific cellular locations of members of the stathmin family.
PDB ID: 4F61Download
MMDB ID: 101359
PDB Deposition Date: 2012/5/14
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 4.17  Å
Source Organism:
Ovis aries
Similar Structures:
Biological Unit for 4F61: nonameric; determined by author and by software (PISA)
Molecular Components in 4F61
Label Count Molecule
Proteins (9 molecules)
4
Tubulin Alpha Chain
Molecule annotation
4
Tubulin Beta Chain
Molecule annotation
1
Stathmin-like Domain R4
Molecule annotation
Chemicals (12 molecules)
1
4
2
4
3
4
* Click molecule labels to explore molecular sequence information.

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