Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carbone V, Schofield LR, Beattie AK, Sutherland-Smith AJ, Ronimus RS. The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium. Proteins. 2013 Nov;81(11):2064-70. doi: 10.1002/prot.24372. Epub 2013 Aug 23. PMID:23873651 doi:http://dx.doi.org/10.1002/prot.24372
