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The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium
Author(s) -
Carbone Vincenzo,
Schofield Linley R.,
Beattie Amy K.,
SutherlandSmith Andrew J.,
Ronimus Ron S.
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24372
Subject(s) - trimer , archaea , stereochemistry , c terminus , biochemistry , sequence (biology) , hydrolase , chemistry , peptide sequence , biology , protein structure , enzyme , amino acid , dimer , gene , organic chemistry
Methenyltetrahydromethanopterin cyclohydrolase (Mch) is involved in the methanogenesis pathway of archaea as a C 1 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. Proteins 2013; 81:2064–2070. © 2013 Wiley Periodicals, Inc.