Crystal structure of YdcE protein from Bacillus subtilis.
نویسندگان
چکیده
Arhonda Gogos, Haiyan Mu, Fabiana Bahna, Carlos A. Gomez, and Lawrence Shapiro Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, New York Department of Ophthalmology, Columbia University College of Physicians and Surgeons, New York, New York Naomi Berrie Diabetes Center, Columbia University College of Physicians and Surgeons, New York, New York
منابع مشابه
The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli, confirms the structural basis for oligomer diversity.
The tautomerase superfamily consists of three major families represented by 4-oxalocrotonate tautomerase (4-OT), 5-(carboxymethyl)-2-hydroxymuconate isomerase (CHMI), and macrophage migration inhibitory factor (MIF). The members of this superfamily are structurally homologous proteins constructed from a simple beta-alpha-beta fold that share a key mechanistic feature; they use an amino-terminal...
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عنوان ژورنال:
- Proteins
دوره 53 2 شماره
صفحات -
تاریخ انتشار 2003