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Shimoni-Livny L , Carrell HL , Wagner T , Kaufman Katz A , Afshar C , Mitchell LW , Volin M , Jaffe EK , Glusker JP
Crystallization and preliminary X-ray diffraction studies of E. coli porphobilinogen synthase and its heavy-atom derivatives
Acta Crystallogr D Biol Crystallogr. 1998 May 1;54 ( Pt 3) :438-40
PMID: 9761921 URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9761921
AbstractPorphobilinogen synthase (PBGS) catalyzes the condensation of two identical substrate molecules, 5-aminolevulinic acid (ALA), in an asymmetric manner to form porphobilinogen. E. coli PBGS is an homooctameric enzyme. The number of active sites is not clear, but each subunit binds one ZnII ion and one MgII ion. Diffraction-quality crystals of native E. coli PBGS have been obtained, and unit-cell dimensions (a = 130.8, c = 144.0 A) are reported. These crystals diffract to about 3.0 A resolution.
Notes98437548 0907-4449 Journal Article