1p9n

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spinqualitylabelsall models 1p9n, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 SO4 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

Page seeded by OCA on Tue Nov 20 23:36:56 2007