Format

Send to

Choose Destination
See comment in PubMed Commons below
Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):419-21.

Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the Pb(II)-complexed enzyme.

Author information

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

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.

PMID:
15299718
DOI:
10.1107/S0907444995013163
[PubMed]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Loading ...
    Support Center