4FIO

Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium

4FIO の概要

• エントリーDOI: 10.2210/pdb4fio/pdb
• 関連するPDBエントリー: 1QLM
• 分子名称: Methenyltetrahydromethanopterin cyclohydrolase, ETHYL ACETATE, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: methanogenesis, hydrolysis, hydrolase
• 由来する生物種: Methanobrevibacter ruminantium
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 113582.05

構造登録者

Carbone, V.,Schofield, L.R.,Beattie, A.K.,Sutherland-Smith, A.J.,Ronimus, R.S. (登録日: 2012-06-10, 公開日: 2013-07-24, 最終更新日: 2023-09-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.37 Å)