Heart Disease Weekly
Welcome to NewsRx!
Learn more about a six-week, no-risk free trial of Heart Disease Weekly
We're a pay-per-view site for premium content. If you'd like to purchase this article, it's only $3.00.
Heart Disease
Studies from University of Sydney describe new findings in heart disease
July 6th, 2008
"The crystal structure of GcnA, an N-acetyl-beta-D-ghlCosaminidase from Streptococcus gordonii, was solved by multiple wavelength anomalous dispersion phasing using crystals of selenomethionine-substituted protein. GcnA is a homodimer with subunits each comprised of three domains," investigators in Sydney, Australia report. "The structure of the C-terminal alpha-helical domain has not been observed previously and forms a large dimerisation interface. The fold of the N-terminal domain is observed in all structurally related glycosidases although its function is unknown. The central domain has a canonical (beta/alpha)(8) TIM-barrel fold which harbours the active site. The...
Source: Heart Disease Weekly (2008-07-06)
|
