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- W42357174 abstract "Holotryptophanase from Proteus vulgaris was crystallized in the presence of K+. The structure was solved at 2.1 Å resolution by molecular replacement technique and refined to descrepancy factor R=15.6%. Each subunit of the tetramer consists of a large and a small domain. The folding of the PLP-binding domain is similar to that of sonic PLP-dependent enzymes. PLP-binding site is formed by two subunits. Potassium ions (one per subunit) arc localized in the interior between two subunits of “cataltical” dimer." @default.
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- W42357174 date "1994-01-01" @default.
- W42357174 modified "2023-09-26" @default.
- W42357174 title "X-ray study of tryptophanase at 2.1 Å resolution" @default.
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- W42357174 doi "https://doi.org/10.1007/978-3-0348-7393-2_29" @default.
- W42357174 hasPublicationYear "1994" @default.
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