Elucidation of the binding of the C1 carrier, tetrahydromethanopterin, and its derivatives, to enzymes involved in the energy metabolism pathway of methanogenic archaea
Final Report Abstract
The aim of this project funded by DFG includes the determination of X-ray structures of H4MPT dependent enzymes of the methanogenic pathway in complex with H4MPT (or derivatives of H4MPT). We succeeded in a ternary complex structure of the two enzymes that provide valuable Informafion ofthe complex ring structure of H4MPT and allowed the postulation of a structure-based enzymatic mechanism. Both studies are either published already or in the revision process. For a third enzyme we have solved the Mch-formyl-H4MPT complex but need better data and also a Mch-methenyl-H4MPT+ structure to publish in a highranking journal. But the data would be already sufficient for a small publication. Mtr is an extremely difficult long-term project where we hoped at the beginning to produce more result. But the "soluble" subunits of the huge membrane protein complex were extremely delicate and a structure determination of MtrA or MtrH was not feasible. However, first promising results of the EM studies exist and a low-resolution structure can be expected in the future (if the project is continuously funded).
Publications
- The structure of a formyl-methanefuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes. J. Mol. Biol. 357, 870-879 (2006)
Acharya, P., Warkentin, E., Ermler, U., Thauer, R.K. & Shima, S.
