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...

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Autores principales:	Caroline Behrens, Beyenech Binotti, Carla Schmidt, Carol V Robinson, John Jia En Chua, Karin Kühnel
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9749ed41526442d68bf7cefd59d985c0
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spelling	oai:doaj.org-article:9749ed41526442d68bf7cefd59d985c02021-11-18T08:53:00ZCrystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation.1932-620310.1371/journal.pone.0076355https://doaj.org/article/9749ed41526442d68bf7cefd59d985c02013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24098481/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The 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.Caroline BehrensBeyenech BinottiCarla SchmidtCarol V RobinsonJohn Jia En ChuaKarin KühnelPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e76355 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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.
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.
format	article
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
title	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_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_sort	crystal structure of the human short coiled coil protein and insights into scoc-fez1 complex formation.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/9749ed41526442d68bf7cefd59d985c0
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_version_	1718421217507016704

Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation.

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