1ZPL

E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me

Summary for 1ZPL

• Entry DOI: 10.2210/pdb1zpl/pdb
• Related: 1O9V
• Descriptor: F17a-G, methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside (3 entities in total)
• Functional Keywords: fimbriae, lectins, bacterial adhesion, protein-sugar complex, cell adhesion
• Biological source: Escherichia coli
• Cellular location: Fimbrium: Q99003
• Total number of polymer chains: 2
• Total formula weight: 38566.92

Authors

Buts, L.,Wellens, A.,Van Molle, I.,Wyns, L.,Loris, R.,Lahmann, M.,Oscarson, S.,De Greve, H.,Bouckaert, J. (deposition date: 2005-05-17, release date: 2006-05-23, Last modification date: 2024-10-30)

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

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: 16041081
DOI: 10.1107/S0907444905017038

Experimental method

X-RAY DIFFRACTION (1.7 Å)