Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli

Lilian Hor; Renwick C J Dobson; Con Dogovski; Craig A Hutton; Matthew A Perugini

doi:10.1107/S1744309109047708

Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):37-40. doi: 10.1107/S1744309109047708. Epub 2009 Dec 25.

Authors

Lilian Hor¹, Renwick C J Dobson, Con Dogovski, Craig A Hutton, Matthew A Perugini

Affiliation

¹ School of Chemistry, The University of Melbourne, Parkville, Victoria 3010, Australia.

Abstract

Diaminopimelate (DAP) epimerase (EC 5.1.1.7) catalyzes the penultimate step of lysine biosynthesis in bacteria and plants, converting L,L-diaminopimelate to meso-diaminopimelate. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DAP epimerase from Escherichia coli are presented. Crystals were obtained in space group P4(1)2(1)2 and diffracted to 2.0 A resolution, with unit-cell parameters a = b = 89.4, c = 179.6 A. Molecular replacement was conducted using Bacillus anthracis DAP epimerase as a search model and showed the presence of two molecules in the asymmetric unit, with an initial R(free) of 0.456 and R(work) of 0.416.

Publication types

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

MeSH terms

Amino Acid Isomerases / chemistry*
Amino Acid Isomerases / isolation & purification
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Escherichia coli / enzymology

Substances

Amino Acid Isomerases
diaminopimelate epimerase