1FTR
FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI
1FTR の概要
| エントリーDOI | 10.2210/pdb1ftr/pdb |
| 分子名称 | FORMYLMETHANOFURAN\:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE (2 entities in total) |
| 機能のキーワード | formyltransferase, methanogenesis, archae, acyltransferase, hyperthermophilic, halophilic |
| 由来する生物種 | Methanopyrus kandleri |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 126745.80 |
| 構造登録者 | Ermler, U.,Merckel, M.C.,Thauer, R.K.,Shima, S. (登録日: 1997-09-21, 公開日: 1998-10-14, 最終更新日: 2024-02-07) |
| 主引用文献 | Ermler, U.,Merckel, M.,Thauer, R.,Shima, S. Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability. Structure, 5:635-646, 1997 Cited by PubMed Abstract: Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the methanogenic Archaeon Methanopyrus kandleri (optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The enzyme is involved in the pathway of carbon dioxide reduction to methane and catalyzes the transfer of formyl from formylmethanofuran to tetrahydromethanopterin. PubMed: 9195883DOI: 10.1016/S0969-2126(97)00219-0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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