1u6i
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(New page: 200px<br /><applet load="1u6i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u6i, resolution 2.20Å" /> '''The Structure of nat...)
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Revision as of 01:45, 21 November 2007
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The Structure of native coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase at 2.2A resolution
Overview
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.
About this Structure
1U6I is a Single protein structure of sequence from Methanopyrus kandleri with MG as ligand. Active as Methylenetetrahydromethanopterin dehydrogenase, with EC number 1.5.99.9 Full crystallographic information is available from OCA.
Reference
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
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