The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri
- Grabarse, Wolfgang
- Vaupel, Martin
- Vorholt, Julia A
- Shima, Seigo
- Thauer, Rudolf K
- Wittershagen, Axel
- Bourenkov, Gleb
- Bartunik, Hans D
- Ermler, Ulrich
DOIAbstract
The reduction of carbon dioxide to methane in methanogenic archaea involves the tetrahydrofolate analogue tetrahydromethanopterin (H4MPT) as a C1 unit carrier. In the third step of this reaction sequence, N5-formyl-H4MPT is converted to methenyl-H4MPT+ by the enzyme methenyltetrahydromethanopterin cyclohydrolase. The cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri (Mch) is extremely thermostable and adapted to a high intracellular concentration of lyotropic salts
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