title: 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 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.
authors.affiliation: AgResearch Limited, Grasslands Research Centre, Tennent Drive, Private Bag 11008, Palmerston North, 4442, New Zealand.
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Carbone
authors.forename: Linley R
authors.initials: LR
authors.lastname: Schofield
authors.forename: Amy K
authors.initials: AK
authors.lastname: Beattie
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Sutherland-Smith
authors.forename: Ron S
authors.initials: RS
authors.lastname: Ronimus
mesh_terms: D000619:Aminohydrolases / Q000737:chemistry*; D019843:Archaeal Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D041581:Methanobrevibacter / Q000201:enzymology*
chemical_list: D019843:Archaeal Proteins; D000619:Aminohydrolases; C050675:methenyltetrahydromethanopterin cyclohydrolase
keywords: archaea; autotroph; coenzyme synthesis; cyclohydrolase; methanogenesis; trimer