Crystallization and preliminary X-ray diffraction studies of E. coli porphobilinogen synthase and its heavy-atom derivatives

L Shimoni-Livny; H L Carrell; T Wagner; A Kaufman Katz; C Afshar; L W Mitchell; M Volin; E K Jaffe; J P Glusker

doi:10.1107/s0907444997010925

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. doi: 10.1107/s0907444997010925.

Authors

L Shimoni-Livny¹, H L Carrell, T Wagner, A Kaufman Katz, C Afshar, L W Mitchell, M Volin, E K Jaffe, J P Glusker

Affiliation

¹ Institute for Cancer Research, Fox Chase Cancer Center, 7701 Burholme Avenue, Philadelphia, PA 19111, USA.

PMID: 9761921
DOI: 10.1107/s0907444997010925

Abstract

Porphobilinogen 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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Crystallization
Escherichia coli / enzymology*
Molecular Weight
Porphobilinogen Synthase / chemistry*
Software
X-Ray Diffraction

Substances

Porphobilinogen Synthase

Abstract

Publication types

MeSH terms

Substances

Grants and funding