 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ir5044fig1mag.jpg)
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Figure 1
Structure of L. pneumophila PDF. (a) Monomeric assembly of L. pneumophila peptide deformylase (LpPDF) bound to Ni2+ (small sphere) and Cl− (large sphere) (PDB entry 6caz). Secondary-structure elements are labeled along with the N- and C- termini. (b) The active site of LpPDF is shown with significant residues represented as sticks and Ni2+ and Cl− ions shown as green spheres. A composite omit map contoured at 4σ is shown around the bound ions. Bold labeled residues coordinate the metal ions, while the others are involved in substrate recognition or catalysis. Bonds to the metal ions are shown as dotted green lines. A MES molecule from the crystallization condition is also bound in the active site (green sticks). (c) UV elution profile of LpPDF from a size-exclusion chromatography (SEC) column. The dotted line designates the peak associated with LpPDF at an elution volume of 69.85 ml. (d) Calibration curve for the SEC column (black circles; A, aprotinin, 6.5 kDa, R, RNaseA, 13.7 kDa; CA, carbonic anhydrase, 29 kDa; C, conalbumin, 75 kDa) and calculated molecular weight of LpPDF (green arrow). (e) Overlay of LpPDF (PDB entry 6caz; green) with the structures of PDFs from E. coli (PDB entry 2w3t; yellow) and H. influenzae (PDB entry 4wxk; blue). (f) Overlay of LpPDF (PDB entry 6caz; green) with substrate Met-Ala-Ser from the substrate-bound structure of E. coli PDF (PDB entry 1bs8; yellow). |
![[Figure 1]](ir5044fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
