Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation.
The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta 1 (FEZ1). This complex is involved in autophagy regulation. We determined the crystal structure of the coiled coil domain of human SCOC at 2.7 Å resolution. SCOC forms a parallel left handed coiled co...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24098481/pdf/?tool=EBI |
| _version_ | 1818573357499547648 |
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| author | Caroline Behrens Beyenech Binotti Carla Schmidt Carol V Robinson John Jia En Chua Karin Kühnel |
| author_facet | Caroline Behrens Beyenech Binotti Carla Schmidt Carol V Robinson John Jia En Chua Karin Kühnel |
| author_sort | Caroline Behrens |
| collection | DOAJ |
| description | The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta 1 (FEZ1). This complex is involved in autophagy regulation. We determined the crystal structure of the coiled coil domain of human SCOC at 2.7 Å resolution. SCOC forms a parallel left handed coiled coil dimer. We observed two distinct dimers in the crystal structure, which shows that SCOC is conformationally flexible. This plasticity is due to the high incidence of polar and charged residues at the core a/d-heptad positions. We prepared two double mutants, where these core residues were mutated to either leucines or valines (E93V/K97L and N125L/N132V). These mutations led to a dramatic increase in stability and change of oligomerisation state. The oligomerisation state of the mutants was characterized by multi-angle laser light scattering and native mass spectrometry measurements. The E93V/K97 mutant forms a trimer and the N125L/N132V mutant is a tetramer. We further demonstrate that SCOC forms a stable homogeneous complex with the coiled coil domain of FEZ1. SCOC dimerization and the SCOC surface residue R117 are important for this interaction. |
| first_indexed | 2024-12-15T00:10:05Z |
| format | Article |
| id | doaj.art-9749ed41526442d68bf7cefd59d985c0 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-15T00:10:05Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-9749ed41526442d68bf7cefd59d985c02022-12-21T22:42:36ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-01810e7635510.1371/journal.pone.0076355Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation.Caroline BehrensBeyenech BinottiCarla SchmidtCarol V RobinsonJohn Jia En ChuaKarin KühnelThe short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta 1 (FEZ1). This complex is involved in autophagy regulation. We determined the crystal structure of the coiled coil domain of human SCOC at 2.7 Å resolution. SCOC forms a parallel left handed coiled coil dimer. We observed two distinct dimers in the crystal structure, which shows that SCOC is conformationally flexible. This plasticity is due to the high incidence of polar and charged residues at the core a/d-heptad positions. We prepared two double mutants, where these core residues were mutated to either leucines or valines (E93V/K97L and N125L/N132V). These mutations led to a dramatic increase in stability and change of oligomerisation state. The oligomerisation state of the mutants was characterized by multi-angle laser light scattering and native mass spectrometry measurements. The E93V/K97 mutant forms a trimer and the N125L/N132V mutant is a tetramer. We further demonstrate that SCOC forms a stable homogeneous complex with the coiled coil domain of FEZ1. SCOC dimerization and the SCOC surface residue R117 are important for this interaction.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24098481/pdf/?tool=EBI |
| spellingShingle | Caroline Behrens Beyenech Binotti Carla Schmidt Carol V Robinson John Jia En Chua Karin Kühnel Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation. PLoS ONE |
| title | Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation. |
| title_full | Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation. |
| title_fullStr | Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation. |
| title_full_unstemmed | Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation. |
| title_short | Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation. |
| title_sort | crystal structure of the human short coiled coil protein and insights into scoc fez1 complex formation |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24098481/pdf/?tool=EBI |
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