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Structural insight into the cooperation of chloroplast chaperonin subunits
Zhang, SJ; Zhou, H; Yu, F; Bai, CC; Zhao, Q; He, JH; Liu, CM; Liu, CM (reprint author), Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Cell & Chromosome Engn, Beijing 100101, Peoples R China.
2016
Source PublicationBMC BIOLOGY
ISSN1741-7007
Volume14Issue:-Pages:
Subtype期刊文献
AbstractBackground: Chloroplast chaperonin, consisting of multiple subunits, mediates folding of the highly abundant protein Rubisco with the assistance of co-chaperonins. ATP hydrolysis drives the chaperonin allosteric cycle to assist substrate folding and promotes disassembly of chloroplast chaperonin. The ways in which the subunits cooperate during this cycle remain unclear. Results: Here, we report the first crystal structure of Chlamydomonas chloroplast chaperonin homo-oligomer (CPN60 beta 1) at 3.8 angstrom, which shares structural topology with typical type I chaperonins but with looser compaction, and possesses a larger central cavity, less contact sites and an enlarged ATP binding pocket compared to GroEL. The overall structure of Cpn60 resembles the GroEL allosteric intermediate state. Moreover, two amino acid (aa) residues (G153, G154) conserved among Cpn60s are involved in ATPase activity regulated by co-chaperonins. Domain swapping analysis revealed that the monomeric state of CPN60 alpha is controlled by its equatorial domain. Furthermore, the C-terminal segment (aa 484-547) of CPN60 beta influenced oligomer disassembly and allosteric rearrangement driven by ATP hydrolysis. The entire equatorial domain and at least one part of the intermediate domain from CPN60 alpha are indispensable for functional cooperation with CPN60 beta 1, and this functional cooperation is strictly dependent on a conserved aa residue (E461) in the CPN60 alpha subunit. Conclusions: The first crystal structure of Chlamydomonas chloroplast chaperonin homo-oligomer (CPN60 beta 1) is reported. The equatorial domain maintained the monomeric state of CPN60 alpha and the C-terminus of CPN60 beta affected oligomer disassembly driven by ATP. The cooperative roles of CPN60 subunits were also established.
KeywordFolding Functional Form Crystal-structure Arabidopsis-thaliana Polypeptide Binding Angstrom Resolution Ii Chaperonins Protein Groel Complexes Atp
DOI10.1186/s12915-016-0251-8
Indexed BySCI
Language英语
WOS IDWOS:000373758200001
Citation statistics
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/25842
Collection中科院上海应用物理研究所2011-2018年
Corresponding AuthorLiu, CM (reprint author), Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Cell & Chromosome Engn, Beijing 100101, Peoples R China.
Recommended Citation
GB/T 7714
Zhang, SJ,Zhou, H,Yu, F,et al. Structural insight into the cooperation of chloroplast chaperonin subunits[J]. BMC BIOLOGY,2016,14(-):—.
APA Zhang, SJ.,Zhou, H.,Yu, F.,Bai, CC.,Zhao, Q.,...&Liu, CM .(2016).Structural insight into the cooperation of chloroplast chaperonin subunits.BMC BIOLOGY,14(-),—.
MLA Zhang, SJ,et al."Structural insight into the cooperation of chloroplast chaperonin subunits".BMC BIOLOGY 14.-(2016):—.
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