4fio | pdb_00004fio

Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium

spinqualitylabelsall models 4fio, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fio is a 3 chain structure with sequence from Metrm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EEE, IPA Related: 1qlm Gene: mch, mru_1619 (METRM) Activity: Methenyltetrahydromethanopterin cyclohydrolase, with EC number 3.5.4.27 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [D3E4S5_METRM] Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+) (By similarity).[HAMAP-Rule:MF_00486] Publication Abstract from PubMed 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 A resolution. A biologically active trimer, the enzyme is composed of two domains including an N-terminal domain of six alpha-helices encompassing a series of four beta-sheets and a predominantly anti-parallel beta-sheet at the C-terminus flanked on one side by alpha-helices. Sequence and structural alignments have helped identify residues involved in substrate binding and trimer formation. The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium.,Carbone V, Schofield LR, Beattie AK, Sutherland-Smith AJ, Ronimus RS Proteins. 2013 Nov;81(11):2064-70. doi: 10.1002/prot.24372. Epub 2013 Aug 23. PMID:23873651 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cyclohydrolase 3D structures

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