2BSB
E. coli F17e-G lectin domain complex with N-acetylglucosamine
Summary for 2BSB
Entry DOI | 10.2210/pdb2bsb/pdb |
Related | 2BSC |
Descriptor | F17G ADHESIN SUBUNIT, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | bacterial adhesion, protein-sugar complex, fimbriae, lectin |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 1 |
Total formula weight | 19158.08 |
Authors | Buts, L.,Wellens, A.,Van Molle, I.,Wyns, L.,Loris, R.,Lahmann, M.,Oscarson, S.,De Greve, H.,Bouckaert, J. (deposition date: 2005-05-20, release date: 2006-05-24, Last modification date: 2024-10-09) |
Primary citation | Buts, L.,Wellens, A.,Van Molle, I.,Wyns, L.,Loris, R.,Lahmann, M.,Oscarson, S.,De Greve, H.,Bouckaert, J. Impact of Natural Variation in Bacterial F17G Adhesins on Crystallization Behaviour. Acta Crystallogr.,Sect.D, 61:1149-, 2005 Cited by PubMed Abstract: 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. PubMed: 16041081DOI: 10.1107/S0907444905017038 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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