1p9n
From Proteopedia
Crystal structure of Escherichia coli MobB.
Structural highlights
Function[MOBB_ECOLI] GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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