Structural highlights
Function
[AROL_DICCH] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Shikimate kinase from Erwinia chrysanthemi, overexpressed in Escherichia coli has been crystallized by the vapour-diffusion method using sodium chloride as a precipitant. Mass spectrometry was used to confirm the purity of the shikimate kinase and dynamic light scattering was used to assess conditions for the monodispersity of the enzyme. The crystals are tetragonal, space group P4(1)2(1)2 or enantiomorph with cell dimensions a = b = 108.5 and c = 92.8 A (at 100 K). Native crystals diffract to better than 2.6 A on a synchrotron X-ray source. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 3.6 A(3) Da(-1).
Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi.,Krell T, Coyle JE, Horsburgh MJ, Coggins JR, Lapthorn AJ Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):612-4. PMID:15299895[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Krell T, Maclean J, Boam DJ, Cooper A, Resmini M, Brocklehurst K, Kelly SM, Price NC, Lapthorn AJ, Coggins JR. Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine. Protein Sci. 2001 Jun;10(6):1137-49. PMID:11369852
- ↑ Krell T, Coyle JE, Horsburgh MJ, Coggins JR, Lapthorn AJ. Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi. Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):612-4. PMID:15299895 doi:10.1107/S0907444997004319
