Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Jun 13;10:2617. doi: 10.1038/s41467-019-10496-3

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 5 — Interaction between RPR and RPPs in MjaRNase P. a Left: The atomic model of the MjaRNase P complex is shown in two orthogonal views. RPPs are color-coded as in Fig. 2a. The two RPR molecules are colored in pink and gray, respectively. Middle: Close-up view of the interface between two RPRs (colored in pink and gray) and the (Pop5-Rpp30)₂ heterotetramer. The two P3 stems are colored in deepteal and green, respectively. Right: Close-up view of the interface between Pop5 and CR-IV of RPR. Pop5 is shown in electrostatic surface representation and RPR in cartoon representation. b Rpp30 simultaneously interacts with the two RPR molecules in the dimeric holoenzyme. One Rpp30 is shown in electrostatic surface representation and the interacting P2-P3 stem from one RPR is colored in deepteal and the other interacting RPR in green. c Close-up view of the interface between the Rpp29-Rpp21-L7Ae heterotrimer and RPR. RPR and RPPs are shown in cartoon and colored as in Fig. 3c and Fig. 2a, respectively