 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](qh5009fig3mag.jpg)
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Figure 3
The catalytic site of Tle1. (a) Structural superposition of the phospholipase catalytic module (cyan) with LipS in complex with spermidine (purple; PDB entry 4fbl ; Chow et al., 2012  ). In the complex structure, the spermidine is remarkably close to the catalytic triad (Ser126, Asp187 and His257) and was thought to mimic substrate bound in the active site. Their similar catalytic sites are boxed and the remarkable inserted helices are labelled. The lid domain in LipS is indicated by an ellipse. (b) The catalytic triad residues Ser235–Asp279–His377 of Tle1 are properly placed to establish hydrogen bonds. (c) Docking model of a phosphatidylglycerol molecule (pink sticks; extracted from PDB entry 4bk2
; Montersino et al., 2013) into the closed conformation of the catalytic pocket composed of D1 (cyan) and part of D3 (orange). Waters found in the active site are depicted as red spheres. (d) Growth of E. coli in agar plates harbouring a vector expressing wild-type Tle1 and its mutants in the periplasm. The cells were prepared with serial tenfold dilutions from left to right. |
![[Figure 3]](qh5009fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
