The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold
We report the crystal structure solution of the Intracellular Protease Inhibitor (IPI) protein from Bacillus subtilis, which has been reported to be an inhibitor of the intracellular subtilisin Isp1 from the same organism. The structure of IPI is a variant of the all-beta, immunoglobulin (Ig) fold....
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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F1000Research
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901451/ https://www.ncbi.nlm.nih.gov/pubmed/24555072 http://dx.doi.org/10.12688/f1000research.2-154.v2 |
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author | Rigden, Daniel J Xu, Qingping Chang, Yuanyuan Eberhardt, Ruth Y Finn, Robert D Rawlings, Neil D |
author_facet | Rigden, Daniel J Xu, Qingping Chang, Yuanyuan Eberhardt, Ruth Y Finn, Robert D Rawlings, Neil D |
author_sort | Rigden, Daniel J |
collection | PubMed |
description | We report the crystal structure solution of the Intracellular Protease Inhibitor (IPI) protein from Bacillus subtilis, which has been reported to be an inhibitor of the intracellular subtilisin Isp1 from the same organism. The structure of IPI is a variant of the all-beta, immunoglobulin (Ig) fold. It is possible that IPI is important for protein-protein interactions, of which inhibition of Isp1 is one. The intracellular nature of ISP is questioned, because an alternative ATG codon in the ipi gene would produce a protein with an N-terminal extension containing a signal peptide. It is possible that alternative initiation exists, producing either an intracellular inhibitor or a secreted form that may be associated with the cell surface. Homologues of the IPI protein from other species are multi-domain proteins, containing signal peptides and domains also associated with the bacterial cell-surface. The cysteine peptidase inhibitors chagasin and amoebiasin also have Ig-like folds, but their topology differs significantly from that of IPI, and they share no recent common ancestor. A model of IPI docked to Isp1 shows similarities to other subtilisin:inhibitor complexes, particularly where the inhibitor interacts with the peptidase active site. |
format | Online Article Text |
id | pubmed-3901451 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | F1000Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-39014512014-01-29 The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold Rigden, Daniel J Xu, Qingping Chang, Yuanyuan Eberhardt, Ruth Y Finn, Robert D Rawlings, Neil D F1000Res Research Article We report the crystal structure solution of the Intracellular Protease Inhibitor (IPI) protein from Bacillus subtilis, which has been reported to be an inhibitor of the intracellular subtilisin Isp1 from the same organism. The structure of IPI is a variant of the all-beta, immunoglobulin (Ig) fold. It is possible that IPI is important for protein-protein interactions, of which inhibition of Isp1 is one. The intracellular nature of ISP is questioned, because an alternative ATG codon in the ipi gene would produce a protein with an N-terminal extension containing a signal peptide. It is possible that alternative initiation exists, producing either an intracellular inhibitor or a secreted form that may be associated with the cell surface. Homologues of the IPI protein from other species are multi-domain proteins, containing signal peptides and domains also associated with the bacterial cell-surface. The cysteine peptidase inhibitors chagasin and amoebiasin also have Ig-like folds, but their topology differs significantly from that of IPI, and they share no recent common ancestor. A model of IPI docked to Isp1 shows similarities to other subtilisin:inhibitor complexes, particularly where the inhibitor interacts with the peptidase active site. F1000Research 2013-08-23 /pmc/articles/PMC3901451/ /pubmed/24555072 http://dx.doi.org/10.12688/f1000research.2-154.v2 Text en Copyright: © 2013 Rigden DJ et al. http://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/publicdomain/zero/1.0/ Data associated with the article are available under the terms of the Creative Commons Zero "No rights reserved" data waiver (CC0 1.0 Public domain dedication). |
spellingShingle | Research Article Rigden, Daniel J Xu, Qingping Chang, Yuanyuan Eberhardt, Ruth Y Finn, Robert D Rawlings, Neil D The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold |
title | The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold |
title_full | The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold |
title_fullStr | The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold |
title_full_unstemmed | The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold |
title_short | The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold |
title_sort | first structure in a family of peptidase inhibitors reveals an unusual ig-like fold |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901451/ https://www.ncbi.nlm.nih.gov/pubmed/24555072 http://dx.doi.org/10.12688/f1000research.2-154.v2 |
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