Xu, L., Muench, S.P., Roujeinikova, A. et al. (2 more authors) (2006) Cloning, purification and preliminary crystallographic analysis of the Bacillus subtilis GTPase YphC-GDP complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F62. pp. 435-437. ISSN 1744-3091
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2006 International Union of Crystallography. Article available Open Access. Article available under the terms of the CC-BY licence. |
Keywords: | GTPase; EngA; YphC |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 06 Jan 2017 11:36 |
Last Modified: | 06 Jan 2017 11:36 |
Published Version: | https://doi.org/10.1107/S1744309106011456 |
Status: | Published |
Publisher: | International Union of Crystallography |
Refereed: | Yes |
Identification Number: | 10.1107/S1744309106011456 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:108135 |