1ho3
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(New page: 200px<br /><applet load="1ho3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ho3, resolution 2.5Å" /> '''CRYSTAL STRUCTURE ANA...)
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Revision as of 14:35, 20 November 2007
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CRYSTAL STRUCTURE ANALYSIS OF E. COLI L-ASPARAGINASE II (Y25F MUTANT)
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
1HO3 is a Single protein structure of sequence from Escherichia coli with ASP as ligand. Active as Asparaginase, 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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