Preliminary structural investigations of the Eut-L shell protein of the ethanolamine ammonia-lyase metabolosome of Escherichia coli.
The ethanolamine ammonia-lyase microcompartment is composed of five different shell proteins that have been proposed to assemble into symmetrically shaped polyhedral particles of varying sizes. Here, preliminary X-ray analysis of crystals of the bacterial microcompartment shell protein Eut-L from Escherichia coli is reported. Cloning, overexpression and purification resulted in highly pure protein that crystallized readily under many different conditions. In all cases the protein forms thin hexagonal plate-shaped crystals belonging to space group P3 that are of unusually high stability against different solvent conditions. The crystals diffracted to a resolution of 2.0 A using synchrotron radiation but proved to be radiation-sensitive. Preparations of heavy-atom-derivatized crystals for use in determining the three-dimensional structure are under way.
Nikolakakis
Kiel
K
Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, California 93106-9510, USA.
Ohtaki
Akashi
A
Newton
Keith
K
Chworos
Arkadiusz
A
Sagermann
Martin
M
D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019856:Ethanolamine / Q000737:chemistry / Q000378:metabolism; D004981:Ethanolamine Ammonia-Lyase / Q000737:chemistry* / Q000378:metabolism; D020815:Polyproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D029968:Escherichia coli Proteins; C541333:EutL protein, E coli; D020815:Polyproteins; D019856:Ethanolamine; D004981:Ethanolamine Ammonia-Lyase