Cargando…
The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1
BACKGROUND: The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question. How Hsp40 co-operates with Hsp70 to facilitate protein folding is not well understood. To investigate the mechanisms, we determined the crystal struc...
Autores principales: | , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2254625/ https://www.ncbi.nlm.nih.gov/pubmed/18211704 http://dx.doi.org/10.1186/1472-6807-8-3 |
_version_ | 1782151208382758912 |
---|---|
author | Hu, Junbin Wu, Yunkun Li, Jingzhi Qian, Xinguo Fu, Zhengqing Sha, Bingdong |
author_facet | Hu, Junbin Wu, Yunkun Li, Jingzhi Qian, Xinguo Fu, Zhengqing Sha, Bingdong |
author_sort | Hu, Junbin |
collection | PubMed |
description | BACKGROUND: The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question. How Hsp40 co-operates with Hsp70 to facilitate protein folding is not well understood. To investigate the mechanisms, we determined the crystal structure of the putative peptide-binding fragment of Hdj1, a human member of the type II Hsp40 family. RESULTS: The 2.7Å structure reveals that Hdj1 forms a homodimer in the crystal by a crystallographic two-fold axis. The Hdj1 dimer has a U-shaped architecture and a large cleft is formed between the two elongated monomers. When compared with another Hsp40 Sis1 structure, the domain I of Hdj1 is rotated by 7.1 degree from the main body of the molecule, which makes the cleft between the two Hdj1 monomers smaller that that of Sis1. CONCLUSION: This structural observation indicates that the domain I of Hsp40 may possess significant flexibility. This flexibility may be important for Hsp40 to regulate the size of the cleft. We propose an "anchoring and docking" model for Hsp40 to utilize the flexibility of domain I to interact with non-native polypeptides and transfer them to Hsp70. |
format | Text |
id | pubmed-2254625 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-22546252008-02-27 The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1 Hu, Junbin Wu, Yunkun Li, Jingzhi Qian, Xinguo Fu, Zhengqing Sha, Bingdong BMC Struct Biol Research Article BACKGROUND: The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question. How Hsp40 co-operates with Hsp70 to facilitate protein folding is not well understood. To investigate the mechanisms, we determined the crystal structure of the putative peptide-binding fragment of Hdj1, a human member of the type II Hsp40 family. RESULTS: The 2.7Å structure reveals that Hdj1 forms a homodimer in the crystal by a crystallographic two-fold axis. The Hdj1 dimer has a U-shaped architecture and a large cleft is formed between the two elongated monomers. When compared with another Hsp40 Sis1 structure, the domain I of Hdj1 is rotated by 7.1 degree from the main body of the molecule, which makes the cleft between the two Hdj1 monomers smaller that that of Sis1. CONCLUSION: This structural observation indicates that the domain I of Hsp40 may possess significant flexibility. This flexibility may be important for Hsp40 to regulate the size of the cleft. We propose an "anchoring and docking" model for Hsp40 to utilize the flexibility of domain I to interact with non-native polypeptides and transfer them to Hsp70. BioMed Central 2008-01-22 /pmc/articles/PMC2254625/ /pubmed/18211704 http://dx.doi.org/10.1186/1472-6807-8-3 Text en Copyright © 2008 Hu et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Hu, Junbin Wu, Yunkun Li, Jingzhi Qian, Xinguo Fu, Zhengqing Sha, Bingdong The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1 |
title | The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1 |
title_full | The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1 |
title_fullStr | The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1 |
title_full_unstemmed | The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1 |
title_short | The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1 |
title_sort | crystal structure of the putative peptide-binding fragment from the human hsp40 protein hdj1 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2254625/ https://www.ncbi.nlm.nih.gov/pubmed/18211704 http://dx.doi.org/10.1186/1472-6807-8-3 |
work_keys_str_mv | AT hujunbin thecrystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT wuyunkun thecrystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT lijingzhi thecrystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT qianxinguo thecrystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT fuzhengqing thecrystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT shabingdong thecrystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT hujunbin crystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT wuyunkun crystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT lijingzhi crystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT qianxinguo crystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT fuzhengqing crystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 AT shabingdong crystalstructureoftheputativepeptidebindingfragmentfromthehumanhsp40proteinhdj1 |