Reference : Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/123126
Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis.
English
Bompard-Gilles, C [> > > >]
Villeret, V [> > > >]
Fanuel, L [> > > >]
Joris, Bernard mailto [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines]
Van Beeumen, J [> > > >]
1999
Acta Crystallographica Section D-Biological Crystallography
Blackwell Publishing
55
Pt 3
699-701
Yes (verified by ORBi)
International
0907-4449
Oxford
United Kingdom
[en] Aminopeptidases/chemistry/metabolism ; Bacterial Proteins ; Crystallization ; Crystallography, X-Ray ; Glycine/chemistry ; Hydrolysis ; Serine/chemistry
[en] Ochrobactrum anthropi possesses an L-aminopeptidase (DmpA) also able to act as a D-amidase/D-esterase. DmpA (40 kDa) is activated by auto-catalyzed protein splicing liberating an alpha-amino group presumably used as a general base in the catalytic mechanism. Two crystal forms were obtained at 294 K in 13-16% PEG 2000 mono-methylether at pH 9.0, adding either 0.2 M magnesium chloride or 1 M lithium chloride. Crystals of the first form belong to the space group C2221 and diffract to 3.0 A resolution, whereas crystals of the second form belong to the space group P21212 and diffract to 2.3 A resolution. Initial screening for heavy-atom derivatives on form II crystals, has led to a well substituted Hg derivative.
http://hdl.handle.net/2268/123126

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