Structural highlights
Function
ASPG_DICCH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.,Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):369-77. PMID:11223513[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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 D Biol Crystallogr. 2001 Mar;57(Pt 3):369-77. PMID:11223513
