1p9n
From Proteopedia
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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
Page seeded by OCA on Thu Feb 21 14:26:37 2008
Categories: Escherichia coli | Single protein | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Cygler, M. | Iannuzzi, P. | Li, Y. | Matte, A. | Rangarajan, S E. | Tocilj, A. | SO4 | Bsgi | Crystal structure | Mobb | Molybdopterin cofactor biosynthesis | Montreal-kingston bacterial structural genomics initiative | Structural genomics
