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

. 2017 Jul 13;7:5312. doi: 10.1038/s41598-017-05509-4

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

© The Author(s) 2017

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

Conformational changes in the CAP subdomain as revealed by structural comparison of PhaC_Cs-CAT and PhaC_Cn-CAT structures. (a) A side-view of the overlay between PhaC_Cs-CAT (cyan and magenta) and PhaC_Cn-CAT (gray and yellow) with an overall r.m.s. deviation of 2.7 Å for Cα carbon atoms. The major conformational deviations are observed in part of the CAP subdomain, the LID region (residues Pro327–Pro386 in magenta) of PhaC_Cs-CAT, which corresponds to the segment Thr355–Pro419 (yellow) of PhaC_Cn-CAT. Arrows indicate conformational transitions of the LID region from PhaC_Cs-CAT to PhaC_Cn-CAT. (b) As in a, but a top-view down to the active site. A narrow path to the active site was found in PhaC_Cn-CAT, whereas the path is covered by the LID region in PhaC_Cs-CAT. (c) To clarify the conformational transitions found by the structural comparison of PhaC_Cs-CAT and PhaC_Cn-CAT, overlay of the LID regions of the two structures are shown. Unfolding of ηA, αA and ηB helices of PhaC_Cs-CAT into a long flexible D-loop found in PhaC_Cn-CAT is indicated by magenta arrows, and refolding of αB’ and ηB’ helices and their linker loop of PhaC_Cs-CAT into a long α4 helix in PhaC_Cn-CAT by red arrows. The disulfide bond between Cys328 and Cys438 of PhaC_Cn-CAT is shown in green.