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• W1504804131 endingPage "2070" @default.
• W1504804131 startingPage "2064" @default.
• W1504804131 abstract "Methenyltetrahydromethanopterin cyclohydrolase (Mch) is involved in the methanogenesis pathway of archaea as a C1 unit carrier where N(5) -formyl-tetrahydromethanopterin is converted to methenyl-tetrahydromethanopterin. Mch from Methanobrevibacter ruminantium was cloned, purified, crystallized and its crystal structure solved at 1.37 Å resolution. A biologically active trimer, the enzyme is composed of two domains including an N-terminal domain of six α-helices encompassing a series of four β-sheets and a predominantly anti-parallel β-sheet at the C-terminus flanked on one side by α-helices. Sequence and structural alignments have helped identify residues involved in substrate binding and trimer formation." @default.
• W1504804131 created "2016-06-24" @default.
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• W1504804131 date "2013-08-23" @default.
• W1504804131 modified "2023-09-26" @default.
• W1504804131 title "The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium" @default.
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• W1504804131 doi "https://doi.org/10.1002/prot.24372" @default.
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