X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase.
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Yoon HJ, Kang KY, Ahn HJ, Shim SM, Ha JY, Lee SK, Mikami B, Suh SW
X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase.
Mol Cells. 2003 Oct 31;16(2):266-9.
- PubMed ID
- 14651272 [ View in PubMed]
- Abstract
The enzyme HemK (or PrmC) is one of the first identified methyltransferases that modify glutamine. It methylates the highly conserved GGQ motif in class I release factors (RF1 and RF2) in Escherichia coli. HemK from Thermotoga maritima was over-expressed and crystallized in the presence of S-adenosylmethionine at 296 K using ammonium sulfate as the precipitant. X-ray diffraction data were collected to 2.5 A resolution from a native crystal. The crystal is orthorhombic, belonging to the space group I222 (or I2(1)2(1)2(1)), with unit-cell parameters of a = 104.24, b = 118.73, and c = 146.62 A. Two (or three) monomers of recombinant HemK are likely to be present in the crystallographic asymmetric unit, giving a V(M) of 3.62 A3 Da(-1) (or 2.41 A3 Da(-1)), with a solvent content of 62.7% (or 44.0%).