4FIO

Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium

Summary for 4FIO

• Entry DOI: 10.2210/pdb4fio/pdb
• Related: 1QLM
• Descriptor: Methenyltetrahydromethanopterin cyclohydrolase, ETHYL ACETATE, ISOPROPYL ALCOHOL, ... (4 entities in total)
• Functional Keywords: methanogenesis, hydrolysis, hydrolase
• Biological source: Methanobrevibacter ruminantium
• Total number of polymer chains: 3
• Total formula weight: 113582.05

Authors

Carbone, V.,Schofield, L.R.,Beattie, A.K.,Sutherland-Smith, A.J.,Ronimus, R.S. (deposition date: 2012-06-10, release date: 2013-07-24, Last modification date: 2023-09-13)

Primary citation

Carbone, V.,Schofield, L.R.,Beattie, A.K.,Sutherland-Smith, A.J.,Ronimus, R.S.
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium.
Proteins, 81:2064-2070, 2013

PubMed 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.

PubMed: 23873651
DOI: 10.1002/prot.24372

Experimental method

X-RAY DIFFRACTION (1.37 Å)