1hfk: Difference between revisions

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{{STRUCTURE_1hfk|  PDB=1hfk  |  SCENE=  }}  
{{STRUCTURE_1hfk|  PDB=1hfk  |  SCENE=  }}  


'''ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE'''
===ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11223513}}


==About this Structure==
==About this Structure==
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[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 08:07, 1 July 2008

File:1hfk.png

Template:STRUCTURE 1hfk

ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATEASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE

Template:ABSTRACT PUBMED 11223513

About this StructureAbout this Structure

1HFK is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.

ReferenceReference

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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