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The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase

MPS-Authors
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Pilak,  O.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Mamat,  B
external;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254803

Vogt,  S.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Hagemeier,  C. H.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer,  R. K.       
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Shima,  S.       
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Pilak, O., Mamat, B., Vogt, S., Hagemeier, C. H., Thauer, R. K., Shima, S., et al. (2006). The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase. Journal of Molecular Biology, 358(3), 798-809. doi:10.1016/j.jmb.2006.02.035.


Cite as: https://hdl.handle.net/21.11116/0000-000F-B394-F
Abstract
The iron-sulphur cluster-free hydrogenase (Hmd, EC 1.12.98.2) from
methanogenic archaea is a novel type of hydrogenase that 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. We report here on the crystal
structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at
1.75 angstrom and from Methanopyrus kandleri at 2.4 angstrom resolution.
Homodimeric Hmd reveals a unique architecture composed of one central
and two identical peripheral globular units. The central unit is
composed of the intertwined C-terminal segments of both subunits,
forming a novel intersubunit fold. The two peripheral units consist of
the N-terminal domain of each subunit. The Rossmann fold-like structure
of the N-terminal domain contains a mononucleotide-binding site, which
could harbour the GMP moiety of the cofactor. Another binding site for
the iron-containing cofactor is most probably Cys176, which is located
at the bottom of a deep intersubunit cleft and which has been shown to
be essential for enzyme activity. Adjacent to the iron of the cofactor
modelled as a ligand to Cys176, an extended U-shaped extra electron
density, interpreted as a polyethyleneglycol fragment, suggests a
binding site for the substrate methenyltetrahydromethanopterin. (c) 2006
Elsevier Ltd. All rights reserved.