1P9N

Crystal structure of Escherichia coli MobB.

Summary for 1P9N

• Entry DOI: 10.2210/pdb1p9n/pdb
• Descriptor: Molybdopterin-guanine dinucleotide biosynthesis protein B, SULFATE ION (3 entities in total)
• Functional Keywords: molybdopterin cofactor biosynthesis, mobb, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, biosynthetic protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 38460.61

Authors

Rangarajan, S.E.,Tocilj, A.,Li, Y.,Iannuzzi, P.,Matte, A.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2003-05-12, release date: 2003-05-20, Last modification date: 2024-10-30)

Primary citation

Rangarajan, S.E.,Tocilj, A.,Li, Y.,Iannuzzi, P.,Matte, A.,Cygler, M.
Molecules of Escherichia coli MobB assemble into densely packed hollow cylinders in a crystal lattice with 75% solvent content.
Acta Crystallogr.,Sect.D, 59:2348-2352, 2003

PubMed 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.

PubMed: 14646116
DOI: 10.1107/S090744490301967X

Experimental method

X-RAY DIFFRACTION (2.8 Å)