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Carrell HL , Glusker JP , Shimoni L , Keefe LJ , Afshar C , Volin M , Jaffe EK
Crystallization and preliminary X-ray diffraction studies of 5- chlorolevulinate-modified bovine porphobilinogen synthase and the Pb-II-complexed enzyme
Acta Crystallographica Section D-Biological Crystallography. 1996 Mar 1;52 :419-421
PMID: ISI:A1996UF18600023   
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Abstract
Bovine porphobilinogen synthase (PBGS) is an homooctameric enzyme with four active sites. Each active site binds two -Zn- II atoms whose ligands differ and two molecules of 5- aminolevulinate whose chemical fates differ. The asymmetric binding of two Zn-II atoms and two identical substrate molecules by a homodimeric active site is apparently unique. Modification by 5-chlorolevulinate can be used to differentiate the two substrate-binding sites; diffraction-quality crystals of 5-chlorolevulinate-modified PBGS have been obtained. Pb-II can be used to differentiate the two different Zn-II-binding sites; diffraction-quality crystals of the Pb-II complex of PBGS have been obtained. Preliminary diffraction data reveal an I422 space group, in agreement with a general model for the quaternary structure of PBGS.
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Times Cited: 5 English Article 2 UF186 ACTA CRYSTALLOGR D-BIOL CRYST