8J67

Crystal structure of Toxoplasma gondii M2AP

Summary for 8J67

• Entry DOI: 10.2210/pdb8j67/pdb
• Related: 8J64
• Descriptor: MIC2-associated protein (2 entities in total)
• Functional Keywords: toxoplasma gondii, mic2, m2ap, tsr6 domain, structural biology, cell invasion
• Biological source: Toxoplasma gondii
• Total number of polymer chains: 3
• Total formula weight: 59057.98

Authors

Wang, F.F.,Zhang, D.J.,Zhang, S.,Springer, T.A.,Song, G.J. (deposition date: 2023-04-24, release date: 2023-08-30, Last modification date: 2024-10-16)

Primary citation

Zhang, S.,Wang, F.,Zhang, D.,Liu, D.,Ding, W.,Springer, T.A.,Song, G.
Structural insights into MIC2 recognition by MIC2-associated protein in Toxoplasma gondii.
Commun Biol, 6:895-895, 2023

PubMed Abstract: Microneme protein 2 (MIC2) and MIC2-associated protein (M2AP) play crucial roles in the gliding motility and host cell invasion of Toxoplasma gondii. Complex formation between MIC2 and M2AP is required for maturation and transport from the microneme to the parasite surface. Previous studies showed that M2AP associates with the 6 TSR domain of MIC2 (TSR6), but the detailed interaction remains unclear. In this study, we report crystal structures of M2AP alone and in complex with TSR6. TSR domains have an unusually thin, long structure with a layer of intercalated residues on one side. The non-layered side of TSR6 with hotspot residue His-620 at the center binds to M2AP. Remarkably, we show that TSR6 residue Y602 is dynamic; it equilibrates between being part of the layer (the layered state) and in a flipped-out state in the absence of M2AP. However, when bound to M2AP, Y602 shifts to the flipped-out state. Our findings provide insights into the association and stabilization of MIC2-M2AP complex, and may be used to develop new therapies to prevent infections caused by this parasite.

PubMed: 37652989
DOI: 10.1038/s42003-023-05277-0

Experimental method

X-RAY DIFFRACTION (1.81 Å)