PDBsum entry 1zk5

Cell adhesion

PDB id: 1zk5

Contents

Protein chain

172 a.a.

Ligands

NAG

Waters ×229

PDB id:

1zk5

Name:

Cell adhesion

Title:

Escherichia coli f17fg lectin domain complex with n-acetylglucosamine

Structure:

F17g adhesin subunit. Chain: a. Fragment: residues 23-198. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: 377f17g. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.40Å R-factor: 0.185 R-free: 0.201

Authors:

L.Buts,A.Wellens,I.Van Molle,E.De Genst,L.Wyns,R.Loris,M.Lahmann, S.Oscarson,H.De Greve,J.Bouckaert

Key ref:

L.Buts et al. (2005). Impact of natural variation in bacterial F17G adhesins on crystallization behaviour. Acta Crystallogr D Biol Crystallogr, 61, 1149-1159. PubMed id: 16041081 DOI: 10.1107/S0907444905017038

Date:

02-May-05 Release date: 02-May-06

Protein chain

Q9RH91  (F17FG_ECOLX) -  F17f-G fimbrial adhesin from Escherichia coli

Seq: 343 a.a.

Struc: 172 a.a.

DOI no: 10.1107/S0907444905017038

Acta Crystallogr D Biol Crystallogr 61:1149-1159 (2005)

PubMed id: 16041081

Impact of natural variation in bacterial F17G adhesins on crystallization behaviour.

L.Buts, A.Wellens, I.Van Molle, L.Wyns, R.Loris, M.Lahmann, S.Oscarson, H.De Greve, J.Bouckaert.

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.

Selected figure(s)

Figure 2.
Figure 2 DLS size-distribution diagrams of F17a-G showing (a) a monodisperse pattern for the second eluted peak from gel filtration and (b) large aggregates in the first eluted peak. A similar pattern as in (b) is obtained upon aging of the F17a-G solution used in (a). The hydrodynamic radius is displayed on the x axis and each of the ten measurements along the y axis. The intensities for the distributions are indicated by the colours blue (absent) to dark red (most prominent).

Figure 3.
Figure 3 Diffraction patterns of (a) F17a-G in complex with GlcNAc( 1-)OMe extending to 1.7 Å resolution, (b) F17b-G in complex with GlcNAc extending to 2.3 Å resolution and (c) F17e-G in complex with GlcNAc extending to 2.4 Å resolution.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2005, 61, 1149-1159) copyright 2005.

Figures were selected by an automated process.