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Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains
The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types with a wide distribution throughout the three domains of life. The type 1 protein mitoNEET has been shown to fold into a dimer with the signature CDGSH motif binding to a [2Fe-2S] cluster. However, the st...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3174974/ https://www.ncbi.nlm.nih.gov/pubmed/21949752 http://dx.doi.org/10.1371/journal.pone.0024790 |
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author | Lin, Jinzhong Zhang, Liman Lai, Shaomei Ye, Keqiong |
author_facet | Lin, Jinzhong Zhang, Liman Lai, Shaomei Ye, Keqiong |
author_sort | Lin, Jinzhong |
collection | PubMed |
description | The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types with a wide distribution throughout the three domains of life. The type 1 protein mitoNEET has been shown to fold into a dimer with the signature CDGSH motif binding to a [2Fe-2S] cluster. However, the structures of all other types of CISDs were unknown. Here we report the crystal structures of type 3, 4, and 6 CISDs determined at 1.5 Å, 1.8 Å and 1.15 Å resolution, respectively. The type 3 and 4 CISD each contain one CDGSH motif and adopt a dimeric structure. Although similar to each other, the two structures have permutated topologies, and both are distinct from the type 1 structure. The type 6 CISD contains tandem CDGSH motifs and adopts a monomeric structure with an internal pseudo dyad symmetry. All currently known CISD structures share dual iron-sulfur binding modules and a β-sandwich for either intermolecular or intramolecular dimerization. The iron-sulfur binding module, the β-strand N-terminal to the module and a proline motif are conserved among different type structures, but the dimerization module and the interface and orientation between the two iron-sulfur binding modules are divergent. Sequence analysis further shows resemblance between CISD types 4 and 7 and between 1 and 2. Our findings suggest that all CISDs share common ancestry and diverged into three primary folds with a characteristic phylogenetic distribution: a eukaryote-specific fold adopted by types 1 and 2 proteins, a prokaryote-specific fold adopted by types 3, 4 and 7 proteins, and a tandem-motif fold adopted by types 5 and 6 proteins. Our comprehensive structural, sequential and phylogenetic analysis provides significant insight into the assembly principles and evolutionary relationship of CISDs. |
format | Online Article Text |
id | pubmed-3174974 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-31749742011-09-26 Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains Lin, Jinzhong Zhang, Liman Lai, Shaomei Ye, Keqiong PLoS One Research Article The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types with a wide distribution throughout the three domains of life. The type 1 protein mitoNEET has been shown to fold into a dimer with the signature CDGSH motif binding to a [2Fe-2S] cluster. However, the structures of all other types of CISDs were unknown. Here we report the crystal structures of type 3, 4, and 6 CISDs determined at 1.5 Å, 1.8 Å and 1.15 Å resolution, respectively. The type 3 and 4 CISD each contain one CDGSH motif and adopt a dimeric structure. Although similar to each other, the two structures have permutated topologies, and both are distinct from the type 1 structure. The type 6 CISD contains tandem CDGSH motifs and adopts a monomeric structure with an internal pseudo dyad symmetry. All currently known CISD structures share dual iron-sulfur binding modules and a β-sandwich for either intermolecular or intramolecular dimerization. The iron-sulfur binding module, the β-strand N-terminal to the module and a proline motif are conserved among different type structures, but the dimerization module and the interface and orientation between the two iron-sulfur binding modules are divergent. Sequence analysis further shows resemblance between CISD types 4 and 7 and between 1 and 2. Our findings suggest that all CISDs share common ancestry and diverged into three primary folds with a characteristic phylogenetic distribution: a eukaryote-specific fold adopted by types 1 and 2 proteins, a prokaryote-specific fold adopted by types 3, 4 and 7 proteins, and a tandem-motif fold adopted by types 5 and 6 proteins. Our comprehensive structural, sequential and phylogenetic analysis provides significant insight into the assembly principles and evolutionary relationship of CISDs. Public Library of Science 2011-09-16 /pmc/articles/PMC3174974/ /pubmed/21949752 http://dx.doi.org/10.1371/journal.pone.0024790 Text en Lin et al. http://creativecommons.org/licenses/by/4.0/ 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 author and source are properly credited. |
spellingShingle | Research Article Lin, Jinzhong Zhang, Liman Lai, Shaomei Ye, Keqiong Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains |
title | Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains |
title_full | Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains |
title_fullStr | Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains |
title_full_unstemmed | Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains |
title_short | Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains |
title_sort | structure and molecular evolution of cdgsh iron-sulfur domains |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3174974/ https://www.ncbi.nlm.nih.gov/pubmed/21949752 http://dx.doi.org/10.1371/journal.pone.0024790 |
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