3F46

The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme from Methanocaldococcus jannaschii

Summary for 3F46

• Entry DOI: 10.2210/pdb3f46/pdb
• Related: 2B0J 3DAF 3DAG 3F47
• Descriptor: 5,10-methenyltetrahydromethanopterin hydrogenase, 5'-O-[(S)-hydroxy{[2-hydroxy-3,5-dimethyl-6-(2-oxoethyl)pyridin-4-yl]oxy}phosphoryl]guanosine, FE (II) ION, ... (6 entities in total)
• Functional Keywords: rossmann fold, helix bundle, complex with iron guanylyl pyridinol cofactor, c176a mutant, methanogenesis, one-carbon metabolism, oxidoreductase
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• Total number of polymer chains: 1
• Total formula weight: 39499.51

Authors

Hiromoto, T.,Vogt, S.,Warkentin, E.,Thauer, R.K.,Shima, S.,Ermler, U. (deposition date: 2008-10-31, release date: 2009-02-10, Last modification date: 2023-11-01)

Primary citation

Hiromoto, T.,Ataka, K.,Pilak, O.,Vogt, S.,Stagni, M.S.,Meyer-Klaucke, W.,Warkentin, E.,Thauer, R.K.,Shima, S.,Ermler, U.
The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex.
Febs Lett., 583:585-590, 2009

PubMed Abstract: [Fe]-hydrogenase is one of three types of enzymes known to activate H(2). Crystal structure analysis recently revealed that its active site iron is ligated square-pyramidally by Cys176-sulfur, two CO, an "unknown" ligand and the sp(2)-hybridized nitrogen of a unique iron-guanylylpyridinol-cofactor. We report here on the structure of the C176A mutated enzyme crystallized in the presence of dithiothreitol (DTT). It suggests an iron center octahedrally coordinated by one DTT-sulfur and one DTT-oxygen, two CO, the 2-pyridinol's nitrogen and the 2-pyridinol's 6-formylmethyl group in an acyl-iron ligation. This result led to a re-interpretation of the iron ligation in the wild-type.

PubMed: 19162018
DOI: 10.1016/j.febslet.2009.01.017

Experimental method

X-RAY DIFFRACTION (1.95 Å)