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The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri

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Grabarse,  Wolfgang
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Max-Planck-Institut für terrestrische Mikrobiologie, 35043 Marburg, Germany;

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Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Grabarse, W., Vaupel, M., Vorholt, J. A., Shima, S., Thauer, R. K., Wittershagen, A., et al. (1999). The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri. Structure, 7(10), 1257-1268. doi:10.1016/s0969-2126(00)80059-3.


Cite as: https://hdl.handle.net/21.11116/0000-0007-6A08-A
Abstract
BACKGROUND:The reduction of carbon dioxide to methane in methanogenic archaea involves the tetrahydrofolate analogue tetrahydromethanopterin (H4MPT) as a C1 unit carrier. In the third step of this reaction sequence, N5-formyl-H4MPT is converted to methenyl-H4MPT+ by the enzyme methenyltetrahydromethanopterin cyclohydrolase. The cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri (Mch) is extremely thermostable and adapted to a high intracellular concentration of lyotropic salts. RESULTS:Mch was crystallized and its structure solved at 2.0 A resolution using a combination of the single isomorphous replacement (SIR) and multiple anomalous dispersion (MAD) techniques. The structure of the homotrimeric enzyme reveals a new alpha/beta fold that is composed of two domains forming a large sequence-conserved pocket between them. Two phosphate ions were found in and adjacent to this pocket, respectively; the latter is displaced by the phosphate moiety of the substrate formyl-H4MPT according to a hypothetical model of the substrate binding. CONCLUSIONS:Although the exact position of the substrate is not yet known, the residues lining the active site of Mch could be tentatively assigned. Comparison of Mch with the tetrahydrofolate-specific cyclohydrolase/dehydrogenase reveals similarities in domain arrangement and in some active-site residues, whereas the fold appears to be different. The adaptation of Mch to high salt concentrations and high temperatures is reflected by the excess of acidic residues at the trimer surface and by the higher oligomerization state of Mch compared with its mesophtic counterparts.