1u6j

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(New page: 200px<br /><applet load="1u6j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u6j, resolution 2.40&Aring;" /> '''The Structure of nat...)
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[[Image:1u6j.gif|left|200px]]<br /><applet load="1u6j" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u6j, resolution 2.40&Aring;" />
caption="1u6j, resolution 2.40&Aring;" />
'''The Structure of native coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase at 2.4A resolution'''<br />
'''The Structure of native coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase at 2.4A resolution'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1U6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylenetetrahydromethanopterin_dehydrogenase Methylenetetrahydromethanopterin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.9 1.5.99.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U6J OCA].
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1U6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylenetetrahydromethanopterin_dehydrogenase Methylenetetrahydromethanopterin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.9 1.5.99.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6J OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ermler, U.]]
[[Category: Ermler, U.]]
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[[Category: Hagemeier, C.H.]]
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[[Category: Hagemeier, C H.]]
[[Category: Shima, S.]]
[[Category: Shima, S.]]
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[[Category: Thauer, R.K.]]
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[[Category: Thauer, R K.]]
[[Category: Warkentin, E.]]
[[Category: Warkentin, E.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: monomer: alpha/beta domain]]
[[Category: monomer: alpha/beta domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:52:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:07 2008''

Revision as of 13:21, 21 February 2008


1u6j, resolution 2.40Å

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

1U6J is a Single protein structure of sequence from Methanopyrus kandleri with 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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