Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 DOI10.2210/pdb6hux/pdb
DescriptorH(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein MJ1338, ACETATE ION, iron-guanylyl pyridinol cofactor, ... (10 entities in total)
Functional Keywordshydrogenase, h2-activation, lateral gene-transfer, cofactor biosynthesis, tetrahydromethanopterin, paralog, methanogen, metalloenzyme, oxidoreductase
Biological sourceMethanocaldococcus jannaschii DSM 2661 (Methanococcus jannaschii)
Total number of polymer chains1
Total formula weight43610.64
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 citationWatanabe, 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: 30600878
DOI: 10.1002/anie.201813465
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

240971

数据于2025-08-27公开中

PDB statisticsPDBj update infoContact PDBjnumon