PGRP-SA Structure and Sequence Comparisons

<div><p>(A) Ribbon diagram showing the front view (left) and side view (right) of PGRP-SA. The ribbon is colored from N to C terminus in a progression from blue to red. Disulfide bridges are shown as sticks. The π helix turn at the end of the H2 helix is indicated.</p> <p>(B) Comparison of PGRP-SA (blue coil, from N to C) and PGRP-LB (green coil, from N′ to C′). (A) and (B) were prepared with Bobscript (<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0020277#pbio-0020277-Esnouf1" target="_blank">Esnouf 1999</a>), GL_RENDER (E. Esser, personal communication), and POV-Ray (Persistence of Vision Ray Tracer v3.1g).</p> <p>(C) Aligned sequences of selected PGRP domains, with a serine and a histidine at position 158 and position 42 of PGRP-SA (marked with asterisks), respectively, from <i>Drosophila</i> (d), mouse (m), and human (h). Secondary-structure elements in PGRP-SA are indicated above the alignment. Invariant residues are boxed in black and colored in white, conserved residues are shaded in yellow, and those lining the putative PG docking groove are in pink. The disulfide bond-forming Cys residues are boxed in gray. The residue number of PGRP-SA is shown above the alignment. The residues chosen for mutagenesis are marked with black circles. A structurally based alignment of the dPGRP-LB sequence is shown at the bottom with its amidase catalytic zinc-coordinating residues colored in red.</p>