PMID:14646116
| Citation |
Rangarajan, SE, Tocilj, A, Li, Y, Iannuzzi, P, Matte, A and Cygler, M (2003) Molecules of Escherichia coli MobB assemble into densely packed hollow cylinders in a crystal lattice with 75% solvent content. Acta Crystallogr. D Biol. Crystallogr. 59:2348-52 |
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| Abstract |
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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| Keywords |
Crystallography, X-Ray; Dimerization; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Models, Molecular; Protein Structure, Quaternary; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Selenomethionine/chemistry; Solvents; Trans-Activators/chemistry; Trans-Activators/genetics |
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