 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
journal menu
![[Figure 1]](wd5205fig1mag.jpg)
|
|
Figure 1
The complex between Kly18 and the SWFP tetrapeptide. (a) Ribbon-type plot in cross-eyed stereo of Kly18 in the standard MP orientation (Gomis-Rüth et al., 2012  ) showing the regular secondary-structure elements (α-helices as ribbons labelled αA–αC and β-strands as arrows labelled βI–βV). The segment delimiting the S1′ pocket is shown with its constituent parts in blue (Met-turn), orange (S1′ wall-forming segment) and yellow (specificity loop). Residues participating in the binding of the two zinc ions (magenta spheres) are shown with their side chains as tan C atoms and are labelled. The tetrapeptide is shown as a stick model with pink C atoms. The tentative potassium cation is displayed as a purple sphere. (b) Initial OMIT (2Fobs − Fcalc)-type electron density in cross-eyed stereo contoured at 0.8σ above the threshold and centred on the final refined model of the inhibitory tetrapeptide (Ser1-Trp2-Phe3-Pro4). (c) Close-up view of (a) in cross-eyed stereo centred on the active-site cleft. Protein residues participating in delimiting the specificity pocket are shown as sticks with tan C atoms and are labelled if not labelled in (a). Solvent molecules are shown as cyan spheres. The side chain of Leu115 is in a double conformation. (d) Superposition in cross-eyed stereo of Kly18 in the present complex (protein in tan, inhibitor in pink) and in the serendipitous product complexes of its previously described magnesium-depleted (PDB entry 2xs3
; protein in pale green, peptide in dark green) and magnesium-bound (PDB entry 2xs4
; protein in pale blue, peptide in dark blue) forms (Cerdà-Costa et al., 2011). The view is similar to that in (c). The cations correspond to those of the SWFP complex. |
![[Figure 1]](wd5205fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
