Reprogramming an ATP-driven protein machine into a light-gated nanocage
Natural protein assemblies have many sophisticated architectures and functions, creating nanoscale storage containers, motors and pumps1–3. Inspired by these systems, protein monomers have been engineered to self-assemble into supramolecular architectures4 including symmetrical5,6, metal-templated7,...
| Main Authors: | , , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
2013
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859876/ |
| id |
pubmed-3859876 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-38598762014-06-01 Reprogramming an ATP-driven protein machine into a light-gated nanocage Hoersch, Daniel Roh, Soung-Hun Chiu, Wah Kortemme, Tanja Article Natural protein assemblies have many sophisticated architectures and functions, creating nanoscale storage containers, motors and pumps1–3. Inspired by these systems, protein monomers have been engineered to self-assemble into supramolecular architectures4 including symmetrical5,6, metal-templated7,8 and cage-like structures8–10. The complexity of protein machines, however, has made it difficult to create assemblies with both defined structures and controllable functions. Here we report protein assemblies that have been engineered to function as light-controlled nanocontainers. We show that an adenosine-5′-triphosphate (ATP)-driven group II chaperonin11,12, which resembles a barrel with a builtin lid, can be reprogrammed to open and close on illumination with different frequencies of light. By engineering photoswitchable azobenzene-based molecules into the structure, light-triggered changes in interatomic distances in the azobenzene moiety are able to drive large-scale conformational changes of the protein assembly. The different states of the assembly can be visualized with single particle cryo-electron microscopy, and the nanocages can be used to capture and release non-native cargos. Similar strategies switching atomic distances with light could be used to build other controllable nanoscale machines. 2013-11-24 2013-12 /pmc/articles/PMC3859876/ /pubmed/24270642 http://dx.doi.org/10.1038/nnano.2013.242 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Hoersch, Daniel Roh, Soung-Hun Chiu, Wah Kortemme, Tanja |
| spellingShingle |
Hoersch, Daniel Roh, Soung-Hun Chiu, Wah Kortemme, Tanja Reprogramming an ATP-driven protein machine into a light-gated nanocage |
| author_facet |
Hoersch, Daniel Roh, Soung-Hun Chiu, Wah Kortemme, Tanja |
| author_sort |
Hoersch, Daniel |
| title |
Reprogramming an ATP-driven protein machine into a light-gated nanocage |
| title_short |
Reprogramming an ATP-driven protein machine into a light-gated nanocage |
| title_full |
Reprogramming an ATP-driven protein machine into a light-gated nanocage |
| title_fullStr |
Reprogramming an ATP-driven protein machine into a light-gated nanocage |
| title_full_unstemmed |
Reprogramming an ATP-driven protein machine into a light-gated nanocage |
| title_sort |
reprogramming an atp-driven protein machine into a light-gated nanocage |
| description |
Natural protein assemblies have many sophisticated architectures and functions, creating nanoscale storage containers, motors and pumps1–3. Inspired by these systems, protein monomers have been engineered to self-assemble into supramolecular architectures4 including symmetrical5,6, metal-templated7,8 and cage-like structures8–10. The complexity of protein machines, however, has made it difficult to create assemblies with both defined structures and controllable functions. Here we report protein assemblies that have been engineered to function as light-controlled nanocontainers. We show that an adenosine-5′-triphosphate (ATP)-driven group II chaperonin11,12, which resembles a barrel with a builtin lid, can be reprogrammed to open and close on illumination with different frequencies of light. By engineering photoswitchable azobenzene-based molecules into the structure, light-triggered changes in interatomic distances in the azobenzene moiety are able to drive large-scale conformational changes of the protein assembly. The different states of the assembly can be visualized with single particle cryo-electron microscopy, and the nanocages can be used to capture and release non-native cargos. Similar strategies switching atomic distances with light could be used to build other controllable nanoscale machines. |
| publishDate |
2013 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859876/ |
| _version_ |
1612037564396470272 |