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. Author manuscript; available in PMC: 2019 Jul 3.
Published in final edited form as: Structure. 2018 May 17;26(7):936–947.e3. doi: 10.1016/j.str.2018.04.008

Figure 2. Interactions of the Decoration Protein for Capsid Stabilization.

Figure 2.

(A) Model of decoration protein trimer highlighting positions of the β tulip domains (blue) within the assembly.

(B) P74–26 gp87 trimer highlights difference in trimer assembly characterized by a ~20° outward rotation of each of the gp87 trimer subunits (see also Video S2). The N-terminal capsid binding region of both crystal structures is disordered, and is drawn as proportional dotted lines in (B) and (C).

(C) Structure of the λ gpD trimer shows the orientation of gpD from the top of the capsid (left) and rotated 90° to the side (right).