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![[Figure 8]](jb5009fig8mag.jpg)
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Figure 8
Orf11 shows limited sequence similarity and high structural similarity to the PlyCA protein from Streptococcus phage C1. (a) Sequences of the PlyCA GyH domain (residues 1–213) and the Orf11 NTD domain (residues 1–201) were aligned using T-Coffee (Armougom et al., 2006  ), with an identity of 22% and a sequence similarity of 40%. Alignments were displayed using ESPript (Gouet et al., 1999) and similarity was calculated using the Risler matrix (Risler et al., 1988). (b) A superposition of the PlyCA GyH domain and Orf11 NTD structures shows that the proteins adopt similar tertiary folds. The two proteins were superimposed with PyMOL (DeLano, 2002) using Cα positions, with an r.m.s.d. of 3.5 Å over 127 atoms. (c) The conserved catalytic residues of the glucosaminidase domain of GyH are Glu78, Tyr74 and Asn87. The equivalent residues Glu71, Tyr67 and Asn81 in Orf11 NTD appear in similar positions. The residues appear in an electronegative cleft in the protein. The electrostatic potentials of Orf11 NTD were calculated using the APBS plugin in PyMOL. |
![[Figure 8]](jb5009fig8.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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