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Open AccessArticle

Crystal Structures of [Fe]-Hydrogenase from Methanolacinia paynteri Suggest a Path of the FeGP-Cofactor Incorporation Process

1
Microbial Protein Structure Group, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Straße 10, 35043 Marburg, Germany
2
Max Planck Research Group Microbial Metabolism, Max Planck Institute for Marine Microbiology, 28359 Bremen, Germany
*
Author to whom correspondence should be addressed.
Inorganics 2020, 8(9), 50; https://doi.org/10.3390/inorganics8090050
Received: 18 August 2020 / Revised: 10 September 2020 / Accepted: 15 September 2020 / Published: 17 September 2020
[Fe]-hydrogenase (Hmd) catalyzes the reversible heterolytic cleavage of H2, and hydride transfer to methenyl-tetrahydromethanopterin (methenyl-H4MPT+). The iron-guanylylpyridinol (FeGP) cofactor, the prosthetic group of Hmd, can be extracted from the holoenzyme and inserted back into the protein. Here, we report the crystal structure of an asymmetric homodimer of Hmd from Methanolacinia paynteri (pHmd), which was composed of one monomer in the open conformation with the FeGP cofactor (holo-form) and a second monomer in the closed conformation without the cofactor (apo-form). In addition, we report the symmetric pHmd-homodimer structure in complex with guanosine monophosphate (GMP) or guanylylpyridinol (GP), in which each ligand was bound to the protein, where the GMP moiety of the FeGP-cofactor is bound in the holo-form. Binding of GMP and GP modified the local protein structure but did not induce the open conformation. The amino-group of the Lys150 appears to interact with the 2-hydroxy group of pyridinol ring in the pHmd–GP complex, which is not the case in the structure of the pHmd–FeGP complex. Lys150Ala mutation decreased the reconstitution rate of the active enzyme with the FeGP cofactor at the physiological pH. These results suggest that Lys150 might be involved in the FeGP-cofactor incorporation into the Hmd protein in vivo. View Full-Text
Keywords: [Fe]-hydrogenase; FeGP cofactor; guanylylpyridinol; conformational changes; X-ray crystallography [Fe]-hydrogenase; FeGP cofactor; guanylylpyridinol; conformational changes; X-ray crystallography
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MDPI and ACS Style

Huang, G.; Arriaza-Gallardo, F.J.; Wagner, T.; Shima, S. Crystal Structures of [Fe]-Hydrogenase from Methanolacinia paynteri Suggest a Path of the FeGP-Cofactor Incorporation Process. Inorganics 2020, 8, 50. https://doi.org/10.3390/inorganics8090050

AMA Style

Huang G, Arriaza-Gallardo FJ, Wagner T, Shima S. Crystal Structures of [Fe]-Hydrogenase from Methanolacinia paynteri Suggest a Path of the FeGP-Cofactor Incorporation Process. Inorganics. 2020; 8(9):50. https://doi.org/10.3390/inorganics8090050

Chicago/Turabian Style

Huang, Gangfeng; Arriaza-Gallardo, Francisco J.; Wagner, Tristan; Shima, Seigo. 2020. "Crystal Structures of [Fe]-Hydrogenase from Methanolacinia paynteri Suggest a Path of the FeGP-Cofactor Incorporation Process" Inorganics 8, no. 9: 50. https://doi.org/10.3390/inorganics8090050

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