Structural highlights
FunctionMTD_METKA Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe diffraction pattern of native protein crystals of F(420)-dependent methylenetetrahydromethanopterin dehydrogenase from Methanopyrus kandleri shows weak additional reflections compared with the selenomethionine-labelled protein crystals, indicating a doubled c unit-cell parameter. These reflections indicate small reorientations of the hexameric structural units, breaking the translational symmetry. TLS refinement of the selenomethionine-labelled protein structure at 1.55 A resolution revealed an anisotropic rigid-body libration of the hexameric units. The anisotropy is consistent with the static reorientation in the native protein crystals. These results are discussed as related to the crystal packing. The relation between the two structures suggests an analogy to structural changes during certain kinds of phase transitions that have been well studied in inorganic structural chemistry. The structure of F420-dependent methylenetetrahydromethanopterin dehydrogenase: a crystallographic 'superstructure' of the selenomethionine-labelled protein crystal structure.,Warkentin E, Hagemeier CH, Shima S, Thauer RK, Ermler U Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):198-202. Epub 2005, Jan 19. PMID:15681872[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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