Open AccessCloning, purification and preliminary crystallographic analysis of the Bacillus subtilis GTPase YphC–GDP complex
Author(s) -
Xu Ling,
Muench Stephen P.,
Roujeinikova Anna,
Sedelnikova Svetlana E.,
Rice David W.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106011456
Subject(s) - gtpase , bacillus subtilis , crystallography , gtp' , polyethylene glycol , cloning (programming) , chemistry , biology , stereochemistry , bacteria , biochemistry , genetics , computer science , programming language , enzyme
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 P 2 1 2 1 2 1 , 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.