The Bacillus subtilis YphC gene encodes an essential GTPase thought to be involved in ribosome binding and whose protein product may represent a target for the development of a novel antibacterial agent. Sequence analysis reveals that YphC belongs to the EngA family of GTPases, which uniquely contain two adjacent GTP-binding domains. Crystals of a selenomethionine-incorporated YphC-GDP complex have been grown using the hanging-drop vapour-diffusion method and polyethylene glycol as a precipitating agent. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 62.71, b = 65.05, c = 110.61 angstroms, and have one molecule in the asymmetric unit. Data sets at three different wavelengths were collected on a single crystal to 2.5 angstroms resolution at the Daresbury SRS in order to solve the structure by MAD. Ultimately, analysis of YphC in complex with GDP may allow a greater understanding of the EngA family of essential GTPases.
|Pages (from-to)||435 - 437|
|Number of pages||3|
|Journal||Acta Crystallographica. Section F: Structural Biology Communications|
|Issue number||Pt 5|
|Publication status||Published - 2006|
Xu, L., Muench, S. P., Roujeinikova, A., Sedelnikova, S. E., & Rice, D. W. (2006). Cloning, purification and preliminary crystallographic analysis of the Bacillus subtilis GTPase YphC-GDP complex. Acta Crystallographica. Section F: Structural Biology Communications, 62(Pt 5), 435 - 437.