The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium

ABSTRACT Methenyltetrahydromethanopterin cyclohydrolase (Mch) is involved in the methanogenesis pathway of archaea as a C1 unit carrier where N5‐formyl‐tetrahydromethanopterin is converted to methenyl‐tetrahydromethanopterin. Mch from Methanobrevibacter ruminantium was cloned, purified, crystallized...

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Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2013-11, Vol.81 (11), p.2064-2070
Main Authors: Carbone, Vincenzo, Schofield, Linley R., Beattie, Amy K., Sutherland-Smith, Andrew J., Ronimus, Ron S.
Format: Article
Language:English
Subjects:
Aminohydrolases - chemistry
Archaea
Archaeal Proteins - chemistry
autotroph
coenzyme synthesis
Crystallography, X-Ray
cyclohydrolase
Methanobrevibacter - enzymology
Methanobrevibacter ruminantium
methanogenesis
trimer
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Summary:ABSTRACT Methenyltetrahydromethanopterin cyclohydrolase (Mch) is involved in the methanogenesis pathway of archaea as a C1 unit carrier where N5‐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. Proteins 2013; 81:2064–2070. © 2013 Wiley Periodicals, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.24372