1HO3

CRYSTAL STRUCTURE ANALYSIS OF E. COLI L-ASPARAGINASE II (Y25F MUTANT)

Summary for 1HO3

• Entry DOI: 10.2210/pdb1ho3/pdb
• Related: 3ECA 4ECA
• Descriptor: L-ASPARAGINASE II, ASPARTIC ACID (3 entities in total)
• Functional Keywords: asparaginase, leukemia, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P00805
• Total number of polymer chains: 2
• Total formula weight: 69487.82

Authors

Jaskolski, M.,Kozak, M.,Lubkowski, P.,Palm, J.G.,Wlodawer, A. (deposition date: 2000-12-08, release date: 2001-03-07, Last modification date: 2024-10-30)

Primary citation

Jaskolski, M.,Kozak, M.,Lubkowski, J.,Palm, G.,Wlodawer, A.
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.
Acta Crystallogr.,Sect.D, 57:369-377, 2001

PubMed Abstract: 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.

PubMed: 11223513
DOI: 10.1107/S0907444900020175

Experimental method

X-RAY DIFFRACTION (2.5 Å)