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

Experimental method

X-RAY DIFFRACTION (1.95 Å)