1hfk
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(New page: 200px<br /> <applet load="1hfk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hfk, resolution 2.17Å" /> '''ASPARAGINASE FROM E...)
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Revision as of 19:02, 29 October 2007
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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 [[1]], with EC number [3.5.1.1]. 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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