Extended Data Fig. 9: NEPRO has structural homology with Rmp1 from S. Cerevisiae. | Nature Structural & Molecular Biology

Extended Data Fig. 9: NEPRO has structural homology with Rmp1 from S. Cerevisiae.

From: RNase MRP subunit composition and role in 40S ribosome biogenesis

Extended Data Fig. 9

(a) A magnified view of the structure of human RNase P (PDB ID:6AHR) with POP1 shown in light pink. Residue P582 is shown in a stick representation in green61. (b) A magnified view of the predicted structure of RNase MRP highlights the RMP64 and RPP29 interaction. Residue V291 is shown in a stick representation in marine blue. This residue is mutated in a patient with Stickler syndrome. (c) A cartoon representation of the predicted structure of RMP64 that was created using AlphaFold 3 is depicted in wheat and the solved structure of S. cerevisae Rmp1 (PDB ID: 7C7A) shown in brown. An overlay of the structurally similar N-terminal helical bundle is shown to the right.

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