Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.
Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli L-asparaginase and of the native Erwinia chrysanthemi L-asparaginase were obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively. The structures of these highly homologous enzymes were solved by molecular replacement and were refined with data extending to 2.2-2.5 A. These structures were compared with each other, as well as with other L-asparaginase structures previously observed with different crystal packing. It is concluded that the observed phenomenon, which is rare, was most likely to have arisen by chance.
Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland.
M
M
Jaskólski
M
M
Kozak
J
J
Lubkowski
G
G
Palm
A
A
Wlodawer
D000595:Amino Acid Sequence; D001215:Asparaginase / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016974:Dickeya chrysanthemi / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D046911:Macromolecular Substances; D001215:Asparaginase