Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the PbII-complexed enzyme
- 1 March 1996
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 52 (2) , 419-421
- https://doi.org/10.1107/s0907444995013163
Abstract
Bovine porphobilinogen synthase (PBGS) is an homo-octameric 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-chiorolevulinate 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.Keywords
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