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

. 2021 Mar 3;49(6):3109–3126. doi: 10.1093/nar/gkab130

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

© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 2. — Conformational dynamics of the apo human CE GTase domain in comparison with the apo PBCV-1 CE GTase. Top panels (A, C, E) refer to the human GTase (10), and lower panels (B, D, F) refer to the PBCV-1 GTase (28). (A, B) Conformational distributions obtained from cMD simulations. The inter-domain distance was taken as the separation between the centres of mass of the NT and OB domains. Histograms were constructed using the data from all cMD replicates. (C, D) The results of the normal mode analysis, visualizing conformational changes in the protein. The lowest frequency mode relating to the open-close motion is depicted as a porcupine plot, with the arrows representing the direction and amplitude of motion for each residue. (E, F) Salt bridges forming between the OB and NT domains of the GTase upon domain closure.