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Carrell HL, Glusker JP, Shimoni L, et al. Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the Pb(II)-complexed enzyme. Acta Crystallogr D Biol Crystallogr. 1996;52:419-21doi: 10.1107/S0907444995013163.
Carrell, H. L., Glusker, J. P., Shimoni, L., Keefe, L. J., Afshar, C., Volin, M., & Jaffe, E. K. (1996). 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, 52419-21. https://doi.org/10.1107/S0907444995013163
Carrell, H L, et al. "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 vol. 52 (1996): 419-21. doi: https://doi.org/10.1107/S0907444995013163
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 Crystallogr D Biol Crystallogr. 1996 Mar 01;52:419-21. doi: 10.1107/S0907444995013163. PMID: 15299718.
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Acta Crystallogr D Biol Crystallogr. 1996 Mar 01;52:419-21. doi: 10.1107/S0907444995013163.

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

H L Carrell, J P Glusker, L Shimoni, L J Keefe, C Afshar, M Volin, E K Jaffe

Affiliations

  1. Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.

PMID: 15299718 DOI: 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.

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