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Literature summary for 1.12.98.2 extracted from

  • Pilak, O.; Mamat, B.; Vogt, S.; Hagemeier, C.H.; Thauer, R.K.; Shima, S.; Vonrhein, C.; Warkentin, E.; Ermler, U.
    The Crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase (2006), J. Mol. Biol., 358, 798-809.
    View publication on PubMed
Search for more literature for 1.12.98.2

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop or sitting-drop, vapour diffusion method. Crystal structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at 1.75 A resolution Methanocaldococcus jannaschii
hanging-drop or sitting-drop, vapour diffusion method. Crystal structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at 2.4 A resolution Methanopyrus kandleri

Metals/Ions

Metals/Ions Comment Organism Structure
Fe tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulfur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base Methanopyrus kandleri
Fe tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulphur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
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-
-
Methanopyrus kandleri
-
-
-

Cofactor

Cofactor Comment Organism Structure
additional information tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulfur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base Methanocaldococcus jannaschii
additional information tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulfur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base Methanopyrus kandleri