1p9n

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(New page: 200px<br /><applet load="1p9n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9n, resolution 2.80&Aring;" /> '''Crystal structure of...)
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[[Image:1p9n.jpg|left|200px]]<br /><applet load="1p9n" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1p9n.jpg|left|200px]]<br /><applet load="1p9n" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p9n, resolution 2.80&Aring;" />
caption="1p9n, resolution 2.80&Aring;" />
'''Crystal structure of Escherichia coli MobB.'''<br />
'''Crystal structure of Escherichia coli MobB.'''<br />
==Overview==
==Overview==
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The crystal structure of Escherichia coli MobB, an enzyme involved in the, final step of molybdenum-cofactor biosynthesis, forms intertwined dimers., Each molecule consists of two segments and requires the second monomer for, stable folding. Dimerization buries a quarter of the solvent-accessible, area of the monomer. These dimers assemble into a hexagonal lattice with, P6(4)22 symmetry and occupy only approximately 25% of the unit-cell, volume. The symmetry-related dimers associate tightly into a helical, structure with a diameter of 250 A and a pitch of 98 A. Two such helices, are intertwined, shifted by 49 A along the sixfold axis. Within the, crystal, these helices form thin-walled cylinders with an external, diameter of 250 A and an internal diameter of 190 A. Their center is, filled with solvent. These cylinders pack closely together, forming a, hexagonal lattice with the highest possible packing density. This, arrangement of dimers allows extensive intermolecular contacts with 75%, solvent content in the crystal.
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The crystal structure of Escherichia coli MobB, an enzyme involved in the final step of molybdenum-cofactor biosynthesis, forms intertwined dimers. Each molecule consists of two segments and requires the second monomer for stable folding. Dimerization buries a quarter of the solvent-accessible area of the monomer. These dimers assemble into a hexagonal lattice with P6(4)22 symmetry and occupy only approximately 25% of the unit-cell volume. The symmetry-related dimers associate tightly into a helical structure with a diameter of 250 A and a pitch of 98 A. Two such helices are intertwined, shifted by 49 A along the sixfold axis. Within the crystal, these helices form thin-walled cylinders with an external diameter of 250 A and an internal diameter of 190 A. Their center is filled with solvent. These cylinders pack closely together, forming a hexagonal lattice with the highest possible packing density. This arrangement of dimers allows extensive intermolecular contacts with 75% solvent content in the crystal.
==About this Structure==
==About this Structure==
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1P9N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P9N OCA].
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1P9N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9N OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
[[Category: Cygler, M.]]
[[Category: Cygler, M.]]
[[Category: Iannuzzi, P.]]
[[Category: Iannuzzi, P.]]
[[Category: Li, Y.]]
[[Category: Li, Y.]]
[[Category: Matte, A.]]
[[Category: Matte, A.]]
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[[Category: Rangarajan, S.E.]]
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[[Category: Rangarajan, S E.]]
[[Category: Tocilj, A.]]
[[Category: Tocilj, A.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:36:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:37 2008''

Revision as of 12:26, 21 February 2008


1p9n, resolution 2.80Å

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Crystal structure of Escherichia coli MobB.

Overview

The crystal structure of Escherichia coli MobB, an enzyme involved in the final step of molybdenum-cofactor biosynthesis, forms intertwined dimers. Each molecule consists of two segments and requires the second monomer for stable folding. Dimerization buries a quarter of the solvent-accessible area of the monomer. These dimers assemble into a hexagonal lattice with P6(4)22 symmetry and occupy only approximately 25% of the unit-cell volume. The symmetry-related dimers associate tightly into a helical structure with a diameter of 250 A and a pitch of 98 A. Two such helices are intertwined, shifted by 49 A along the sixfold axis. Within the crystal, these helices form thin-walled cylinders with an external diameter of 250 A and an internal diameter of 190 A. Their center is filled with solvent. These cylinders pack closely together, forming a hexagonal lattice with the highest possible packing density. This arrangement of dimers allows extensive intermolecular contacts with 75% solvent content in the crystal.

About this Structure

1P9N is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Molecules of Escherichia coli MobB assemble into densely packed hollow cylinders in a crystal lattice with 75% solvent content., Rangarajan SE, Tocilj A, Li Y, Iannuzzi P, Matte A, Cygler M, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2348-52. Epub 2003, Nov 27. PMID:14646116

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