The Crystal Structure of Methenyltetrahydromethano- Pterin Cyclohydrolase from the Hyperthermophilic Archaeon Methanopyrus Kandleri
Grabarse, W., Vaupel, M., Vorholt, J.A., Shima, S., Thauer, R.K., Wittershagen, A., Bourenkov, G., Bartunik, H.D., Ermler, U.(1999) Structure 7: 1257
- PubMed: 10545331 
- DOI: https://doi.org/10.1016/s0969-2126(00)80059-3
- Primary Citation of Related Structures:  
1QLM - PubMed Abstract: 
The reduction of carbon dioxide to methane in methanogenic archaea involves the tetrahydrofolate analogue tetrahydromethanopterin (H(4)MPT) as a C(1) unit carrier. In the third step of this reaction sequence, N(5)-formyl-H(4)MPT is converted to methenyl-H(4)MPT(+) 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.
Organizational Affiliation: 
Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Strasse, 35043, Marburg, Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Strasse 7, 60528, Frankurt, Germany.