Cloning, purification and preliminary crystallographic analysis of the Bacillus subtilis GTPase YphC-GDP complex

Ling Xu, Stephen P. Muench, Anna Roujeinikova, Svetlana E. Sedelnikova, David W. Rice

    Research output: Contribution to journalArticlepeer-review

    Abstract

    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 P212121, with unit-cell parameters a = 62.71, b = 65.05, c = 110.61 Å, and have one molecule in the asymmetric unit. Data sets at three different wavelengths were collected on a single crystal to 2.5 Å 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. © 2006 International Union of Crystallography. All rights reserved.
    Original languageEnglish
    Pages (from-to)435-437
    Number of pages2
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume62
    Issue number5
    DOIs
    Publication statusPublished - May 2006

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