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- Chumnarnsilpa, Sakesit, 1967-, et al.
(author)
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Activation in isolation : exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin
- 2003
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In: FEBS Letters. - Netherlands : Elsevier Science B.V.. - 0014-5793 .- 1873-3468. ; 552:2-3, s. 82-85
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Journal article (peer-reviewed)abstract
- Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of Ca(2+) ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither actin nor the type-l Ca(2+), which normally is sandwiched between actin and G4, is required to achieve this conformation.
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| 3. |
- Lovelace, Jeffrey J., et al.
(author)
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Protein crystals can be incommensurately modulated
- 2008
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In: Journal of applied crystallography. - 0021-8898 .- 1600-5767. ; 41, s. 600-605
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Journal article (peer-reviewed)abstract
- For a normal periodic crystal, the X-ray diffraction pattern can be described by an orientation matrix and a set of three integers that indicate the reciprocal lattice points. Those integers determine the spacing along the reciprocal lattice directions. In aperiodic crystals, the diffraction pattern is modulated and the standard periodic main reflections are surrounded by satellite reflections. The successful indexing and refinement of the main unit cell and q vector using TWINSOLVE, developed by Svensson [(2003). Lund University, Sweden], are reported here for an incommensurately modulated, aperiodic crystal of a profilin: actin complex. The indexing showed that the modulation is along the b direction in the crystal, which corresponds to an 'actin ribbon' formed by the crystal lattice. Interestingly, the transition to the aperiodic state was shown to be reversible and the diffraction pattern returned to the periodic state during data collection. It is likely that the protein underwent a conformational change that affected the neighbouring profilin: actin molecules in such a way as to produce the observed modulation in the diffraction pattern. Future work will aim to trap the incommensurately modulated crystal state, for example using cryocooling or chemical crosslinking, thus allowing complete X-ray data to be collected.
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