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Wiley, Proteins: Structure, Function, and Bioinformatics, 11(81), p. 2064-2070, 2013

DOI: 10.1002/prot.24372

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The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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, crystallised 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. © Proteins 2013;. © 2013 Wiley Periodicals, Inc.