6HUX

HmdII from Methanocaldococcus jannaschii reconstitued with Fe-guanylylpyridinol (FeGP) cofactor and co-crystallized with methenyl-tetrahydromethanopterin at 2.5 A resolution

Summary for 6HUX

• Entry DOI: 10.2210/pdb6hux/pdb
• Descriptor: H(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein MJ1338, ACETATE ION, iron-guanylyl pyridinol cofactor, ... (10 entities in total)
• Functional Keywords: hydrogenase, h2-activation, lateral gene-transfer, cofactor biosynthesis, tetrahydromethanopterin, paralog, methanogen, metalloenzyme, oxidoreductase
• Biological source: Methanocaldococcus jannaschii DSM 2661 (Methanococcus jannaschii)
• Total number of polymer chains: 1
• Total formula weight: 43610.64

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: 2024-01-24)

• 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; PubMed: 30600878; DOI: 10.1002/anie.201813465

Experimental method

X-RAY DIFFRACTION (2.5 Å)