1ZK5
Escherichia coli F17fG lectin domain complex with N-acetylglucosamine
Summary for 1ZK5
| Entry DOI | 10.2210/pdb1zk5/pdb |
| Related | 1O9V |
| Descriptor | F17G adhesin subunit, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | lectin, beta sandwich, protein-structure complex, immunoglobulin-like fold, cell adhesion |
| Biological source | Escherichia coli |
| Cellular location | Fimbrium (By similarity): Q9RH91 |
| Total number of polymer chains | 1 |
| Total formula weight | 19081.00 |
| Authors | Buts, L.,Wellens, A.,Van Molle, I.,De Genst, E.,Wyns, L.,Loris, R.,Lahmann, M.,Oscarson, S.,De Greve, H.,Bouckaert, J. (deposition date: 2005-05-02, release date: 2006-05-02, Last modification date: 2024-11-20) |
| 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, 61:1149-1159, 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 (1.4 Å) |
Structure validation
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