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

. 2022 Jul 28;13:4370. doi: 10.1038/s41467-022-32086-6

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

© The Author(s) 2022

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. 3 — A superimposition of (a) unbound C. difficile PBP2 (orange) with ampicillin-bound form (green) shows β-lactam binding causes major conformational changes in the active site (top panel) and peripheral regions (bottom panel). Significant movements are indicated by arrows. b By comparing the complex structure of ampicillin (green) with ceftobiprole (purple) we find larger conformational changes in the active site (top panel) and overall (bottom panel) that are consistent with the larger size of the cephem core. c A superimposition of all three structures highlights the global conformation differences in all three structures, with movements mostly localized to the coiled-coil stretch, central-helix cluster, and NTD.