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

Pilak, O., Mamat, B., Vogt, S., Hagemeier, C., Thauer, R., Shima, S., et al. (2006). The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase. Journal of Molecular Biology, 358(3), 798-09. doi:10.1016/j.jmb.2006.02.035.

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Pilak, Oliver1, Author              
Mamat, Björn, Author
Vogt, Sonja1, Author              
Hagemeier, Christoph1, Author              
Thauer, Rudolf2, Author              
Shima, Seigo3, Author              
Vonrhein, Clemens1, Author              
Warkentin, Eberhard, Author
Ermler, Ulrich, Author
Affiliations:
1Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266311              
2Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266289              
3Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              

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 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 A and from Methanopyrus kandleri at 2.4 A 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.

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Language(s): eng - English
 Dates: 2006-05
 Publication Status: Published in print
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 Identifiers: eDoc: 298198
DOI: 10.1016/j.jmb.2006.02.035
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Title: Journal of Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 358 (3) Sequence Number: - Start / End Page: 798 - 09 Identifier: -