6HUY
HmdII from Desulfurobacterium thermolithotrophum reconstitued with Fe-guanylylpyridinol (FeGP) cofactor and co-crystallized with methenyl-tetrahydrofolate form A
Summary for 6HUY
| Entry DOI | 10.2210/pdb6huy/pdb |
| Descriptor | Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein, iron-guanylyl pyridinol cofactor, GLYCEROL, ... (8 entities in total) |
| Functional Keywords | hydrogenase, h2-activation, lateral gene-transfer, cofactor biosynthesis, tetrahydromethanopterin, tetrahydrofolate, paralog, sulfur-reducing bacteria, metalloenzyme, oxidoreductase |
| Biological source | Desulfurobacterium thermolithotrophum DSM 11699 More |
| Total number of polymer chains | 4 |
| Total formula weight | 168287.98 |
| Authors | Watanabe, T.,Wagner, T.,Huang, G.,Kahnt, J.,Ataka, K.,Ermler, U.,Shima, S. (deposition date: 2018-10-09, release date: 2019-01-09, Last modification date: 2024-10-23) |
| Primary citation | Watanabe, T.,Wagner, T.,Huang, G.,Kahnt, J.,Ataka, K.,Ermler, U.,Shima, S. The Bacterial [Fe]-Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates. Angew. Chem. Int. Ed. Engl., 58:3506-3510, 2019 Cited by PubMed Abstract: [Fe]-hydrogenase (Hmd) catalyzes the reversible hydrogenation of methenyl-tetrahydromethanopterin (methenyl-H MPT ) with H . H MPT is a C1-carrier of methanogenic archaea. One bacterial genus, Desulfurobacterium, contains putative genes for the Hmd paralog, termed HmdII, and the HcgA-G proteins. The latter are required for the biosynthesis of the prosthetic group of Hmd, the iron-guanylylpyridinol (FeGP) cofactor. This finding is intriguing because Hmd and HmdII strictly use H MPT derivatives that are absent in most bacteria. We identified the presence of the FeGP cofactor in D. thermolithotrophum. The bacterial HmdII reconstituted with the FeGP cofactor catalyzed the hydrogenation of derivatives of tetrahydrofolate, the bacterial C1-carrier, albeit with low enzymatic activities. The crystal structures show how Hmd recognizes tetrahydrofolate derivatives. These findings have an impact on future biotechnology by identifying a bacterial Hmd paralog. PubMed: 30600878DOI: 10.1002/anie.201813465 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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