Abstract:
:Chorismate pathway enzymes are important as producers of nonnucleotide aromatic compounds. The enzyme chorismate lyase from Escherichia coli has been crystallized in four distinct forms, three of which have been characterized by X-ray diffraction. Despite widespread screening, all four crystal forms grow from the same chemical conditions. The wild-type enzyme tends to aggregate, even in the presence of reducing agent, and yielded only one crystal form (monoclinic, form 1) that grew in intricate clusters. Chemical modification of the cysteines mitigated problems with aggregation and solubility but did not affect crystal growth behavior. Protein aggregation was largely eliminated by mutating the protein's two cysteines to serines. The double mutant retains full enzymatic activity and crystallizes in three new forms, one of which (triclinic) diffracts to 1.1-A resolution.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Stover C,Mayhew MP,Holden MJ,Howard A,Gallagher DTdoi
10.1006/jsbi.1999.4205keywords:
subject
Has Abstractpub_date
2000-02-01 00:00:00pages
96-9issue
1eissn
1047-8477issn
1095-8657pii
S1047-8477(99)94205-3journal_volume
129pub_type
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