2bs7
CRYSTAL STRUCTURE OF F17B-G IN COMPLEX WITH CHITOBIOSE
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OverviewOverview
Since the introduction of structural genomics, the protein has been, recognized as the most important variable in crystallization. Recent, strategies to modify a protein to improve crystal quality have included, rationally engineered point mutations, truncations, deletions and fusions., Five naturally occurring variants, differing in 1-18 amino acids, of the, 177-residue lectin domain of the F17G fimbrial adhesin were expressed and, purified in identical ways. For four out of the five variants crystals, were obtained, mostly in non-isomorphous space groups, with diffraction, limits ranging between 2.4 and 1.1 A resolution. A comparative analysis of, the crystal-packing contacts revealed that the variable amino acids are, often involved in lattice contacts and a single amino-acid substitution, can suffice to radically change crystal packing. A statistical approach, proved reliable to estimate the compatibilities of the variant sequences, with the observed crystal forms. In conclusion, natural variation, universally present within prokaryotic species, is a valuable genetic, resource that can be favourably employed to enhance the crystallization, success rate with considerably less effort than other strategies.
About this StructureAbout this Structure
2BS7 is a Single protein structure of sequence from Escherichia coli with CBS as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Impact of natural variation in bacterial F17G adhesins on crystallization behaviour., Buts L, Wellens A, Van Molle I, Wyns L, Loris R, Lahmann M, Oscarson S, De Greve H, Bouckaert J, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1149-59. Epub 2005, Jul 20. PMID:16041081
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