1HFK

Asparaginase from Erwinia chrysanthemi, hexagonal form with weak sulfate

Summary for 1HFK

• Entry DOI: 10.2210/pdb1hfk/pdb
• Related: 1HFJ 3PGA
• Descriptor: L-ASPARAGINE AMIDOHYDROLASE, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: ERWINIA CHRYSANTHEMI
• Total number of polymer chains: 2
• Total formula weight: 70438.17

Authors

Lubkowski, J.,Palm, G.J.,Kozak, M.,Jaskolski, M.,Wlodawer, A. (deposition date: 2000-12-05, release date: 2000-12-07, Last modification date: 2023-12-13)

Primary citation

Jaskolski, M.,Kozak, M.,Lubkowski, J.,Palm, G.J.,Wlodawer, A.
Structures of Two Highly Homologous Bacterial L-Asparaginases: A Case of Enantiomorphic Space Groups
Acta Crystallogr.,Sect.D, 57:369-, 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 (2.17 Å)