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

. 2013 Jun 11;33(3):e00043. doi: 10.1042/BSR20130017

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

© 2013 The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

(a) CapE forms a hexamer organized as a trimer of dimers (3×2). The structure corresponds to wild-type CapE in complex with substrate analogue (ligand is not shown). The protein subunits of one of the pseudo-dimers are depicted in dark and light blue (chains A and B). The other subunits are depicted in black and grey. (b) SEC profile of CapE. The arrows indicate the elution of the calibration standards. CapE elutes with an apparent molecular weight of 210 kDa. A minor fraction of monomer (8%) with an apparent molecular weight of 40 kDa is also observed. The predicted molecular weight of one subunit of CapE is 39 kDa, and that of the hexamer is 230 kDa. The peak corresponding to the dimer was not observed. (c) Interaction surfaces between protein subunits. The three main contact interfaces correspond to subunits A–B, A–F and A–C. (d) Same interaction surfaces in mutein K126E.