1hfk: Difference between revisions
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==Overview== | ==Overview== | ||
Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Kozak, M.]] | [[Category: Kozak, M.]] | ||
[[Category: Lubkowski, J.]] | [[Category: Lubkowski, J.]] | ||
[[Category: Palm, G | [[Category: Palm, G J.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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Revision as of 11:00, 21 February 2008
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ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE
Overview
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.
About this Structure
1HFK is a Single protein structure of sequence from Erwinia chrysanthemi with SO4 as ligand. Active as Asparaginase, with EC number 3.5.1.1 Known structural/functional Sites: AS1 and AS2. Full crystallographic information is available from OCA.
Reference
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
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