1U6J

The Structure of native coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase at 2.4A resolution

Summary for 1U6J

• Entry DOI: 10.2210/pdb1u6j/pdb
• Related: 1U6I 1U6K 1qv9
• Descriptor: F420-dependent methylenetetrahydromethanopterin dehydrogenase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: monomer: alpha/beta domain, helix bundle; trimer of dimers, oxidoreductase
• Biological source: Methanopyrus kandleri
• Total number of polymer chains: 12
• Total formula weight: 377185.06

Authors

Warkentin, E.,Hagemeier, C.H.,Shima, S.,Thauer, R.K.,Ermler, U. (deposition date: 2004-07-30, release date: 2005-02-01, Last modification date: 2023-08-23)

Primary citation

Warkentin, E.,Hagemeier, C.H.,Shima, S.,Thauer, R.K.,Ermler, U.
The structure of F420-dependent methylenetetrahydromethanopterin dehydrogenase: a crystallographic 'superstructure' of the selenomethionine-labelled protein crystal structure.
Acta Crystallogr.,Sect.D, 61:198-202, 2005

PubMed Abstract: The 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.

PubMed: 15681872
DOI: 10.1107/S0907444904030732

Experimental method

X-RAY DIFFRACTION (2.4 Å)