6huy | pdb_00006huy

HmdII from Desulfurobacterium thermolithotrophum reconstitued with Fe-guanylylpyridinol (FeGP) cofactor and co-crystallized with methenyl-tetrahydrofolate form A

spinqualitylabelsall models 6huy, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6huy is a 4 chain structure with sequence from Destd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DMS, FE9, GOL, GUE, PG4 NonStd Res: CSO Gene: Dester_1504 (DESTD) Activity: 5,10-methenyltetrahydromethanopterin hydrogenase, with EC number 1.12.98.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed [Fe]-hydrogenase (Hmd) catalyzes the reversible hydrogenation of methenyl-tetrahydromethanopterin (methenyl-H4MPT+) with H2. H4MPT is a C1-carrier of methanogenic archaea. One bacterial genus, Desulfurobacterium, contains putative genes for the Hmd paralog (HmdII) and the HcgA-G proteins. The latter are involved in biosynthesis of the prosthetic group of Hmd, the iron-guanylylpyridinol (FeGP) cofactor. This finding is intriguing because Hmd and HmdII strictly use H4MPT 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 enzyme reactions using the tetrahydrofolate derivatives, which are the bacterial C1 carrier, albeit with low enzymatic activities. Crystal structure provided the basis for how the enzyme was adapted to the bacterial C1-carrier. This finding has impact on future biotechnology by developing the Hmd variants functioning in Bacteria. The bacterial [Fe]-hydrogenase paralog uses tetrahydrofolate derivatives as substrates.,Watanabe T, Wagner T, Huang G, Kahnt J, Ataka K, Ermler U, Shima S Angew Chem Int Ed Engl. 2019 Jan 2. doi: 10.1002/anie.201813465. PMID:30600878 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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