Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 류성언 | - |
dc.date.accessioned | 2018-04-12T13:41:01Z | - |
dc.date.available | 2018-04-12T13:41:01Z | - |
dc.date.issued | 2011-12 | - |
dc.identifier.citation | FEBS LETTERS, FEB 18 2011, 585(4), p664-p670, 7p. | en_US |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0014579311000597 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11754/65717 | - |
dc.description.abstract | Heat shock protein 33 (Hsp33) from Escherichia coli is a redox-regulated molecular chaperone that protects cells from oxidative stress. To understand the molecular basis for the monomer-dimer switch in the functional regulation of E. coli Hsp33, we generated a constitutively monomeric Hsp33 by introducing the Q151E mutation in the dimeric interface and determined its crystal structure. The overall scaffold of the monomeric Hsp33(1-235) (Q151E) mutant is virtually the same as that of the dimeric form, except that there is no domain swapping. The measurement of chaperone activity to thermally denatured luciferase showed that the constitutively monomeric Hsp33 mutant still retains chaperone activity similar to that of wild-type Hsp33(1-235), suggesting that a Hsp33 monomer is sufficient to interact with slowly unfolded substrate. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | en_US |
dc.description.sponsorship | This study was supported by Mid-career Researcher Programthrough NRF Grant funded by the MEST (No. 2010-0014305) andWorld Class Institute Program founded by the Korea ResearchFoundation, Ministry of Education, Science and Technology. Thisstudy was also supported by Mid-career Researcher Programthrough NRF grant funded by the MEST (No. 2008-0061624 toS.-W.C.). We thank the staffs of the Pohang Accelerator Laboratorybeamline 6B for help with data collection. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier Science B.V., Amsterdam. | en_US |
dc.subject | Heat shock protein 33 (Hsp33) | en_US |
dc.subject | Chaperone | en_US |
dc.subject | Domain-swapping | en_US |
dc.subject | Redox-sensitive | en_US |
dc.subject | REDOX-REGULATED CHAPERONE | en_US |
dc.subject | HEAT-SHOCK-PROTEIN | en_US |
dc.subject | SWITCH DOMAIN | en_US |
dc.subject | ACTIVATION | en_US |
dc.subject | MECHANISM | en_US |
dc.subject | NETWORK | en_US |
dc.subject | STRESS | en_US |
dc.title | Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity | en_US |
dc.type | Article | en_US |
dc.relation.no | 4 | - |
dc.relation.volume | 585 | - |
dc.identifier.doi | 10.1016/j.febslet.2011.01.029 | - |
dc.relation.page | 664-670 | - |
dc.relation.journal | FEBS LETTERS | - |
dc.contributor.googleauthor | Chi, S. W. | - |
dc.contributor.googleauthor | Jeong, D. G. | - |
dc.contributor.googleauthor | Woo, J. R. | - |
dc.contributor.googleauthor | Lee, H. S. | - |
dc.contributor.googleauthor | Park, B. C. | - |
dc.contributor.googleauthor | Kim, B. Y. | - |
dc.contributor.googleauthor | Erikson, R. L. | - |
dc.contributor.googleauthor | Ryu, S. E. | - |
dc.contributor.googleauthor | Kim, S. J. | - |
dc.relation.code | 2011203177 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF ENGINEERING[S] | - |
dc.sector.department | DEPARTMENT OF BIOENGINEERING | - |
dc.identifier.pid | ryuse | - |
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