1Y60

Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1 with bound 5,10-methylene tetrahydromethanopterin

1Y60 の概要

• エントリーDOI: 10.2210/pdb1y60/pdb
• 関連するPDBエントリー: 1Y5Y
• 分子名称: Formaldehyde-activating enzyme fae, 5,10-DIMETHYLENE TETRAHYDROMETHANOPTERIN (3 entities in total)
• 機能のキーワード: pentamer; beta-alpha-beta left handed crossover; tetrahydromethanopterin-binding, lyase
• 由来する生物種: Methylobacterium extorquens
• 細胞内の位置: Cytoplasm: Q9FA38
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 93835.42

構造登録者

Acharya, P.,Goenrich, M.,Hagemeier, C.H.,Demmer, U.,Vorholt, J.A.,Thauer, R.K.,Ermler, U. (登録日: 2004-12-03, 公開日: 2005-01-11, 最終更新日: 2023-08-23)

主引用文献

Acharya, P.,Goenrich, M.,Hagemeier, C.H.,Demmer, U.,Vorholt, J.A.,Thauer, R.K.,Ermler, U.
How an enzyme binds the C1-carrier tetrahydromethanopterin: Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1
J.Biol.Chem., 280:13712-13719, 2005

PubMed Abstract: Tetrahydromethanopterin (H4 MPT) is a tetrahydrofolate analogue involved as a C1 carrier in the metabolism of various groups of microorganisms. How H4MPT is bound to the respective C1 unit converting enzymes remained elusive. We describe here the structure of the homopentameric formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1 established at 2.0 angstrom without and at 1.9 angstrom with methylene-H4MPT bound. Methylene-H4MPT is bound in an "S"-shaped conformation into the cleft formed between two adjacent subunits. Coenzyme binding is accompanied by side chain rearrangements up to 5 angstrom and leads to a rigidification of the C-terminal arm, a formation of a new hydrophobic cluster, and an inversion of the amide side chain of Gln88. Methylene-H4MPT in Fae shows a characteristic kink between the tetrahydropyrazine and the imidazolidine rings of 70 degrees that is more pronounced than that reported for free methylene-H4MPT in solution (50 degrees). Fae is an essential enzyme for energy metabolism and formaldehyde detoxification of this bacterium and catalyzes the formation of methylene-H4MPT from H4MPT and formaldehyde. The molecular mechanism ofthis reaction involving His22 as acid catalyst is discussed.

PubMed: 15632161
DOI: 10.1074/jbc.M412320200

実験手法

X-RAY DIFFRACTION (1.9 Å)