Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity

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dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorDae Gwin Jeong-
dc.contributor.authorJ R Woo-
dc.contributor.authorHye-Seon Lee-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorBo Yeon Kim-
dc.contributor.authorR L Erikson-
dc.contributor.authorS E Ryu-
dc.contributor.authorSeung Jun Kim-
dc.date.accessioned2017-04-19T09:22:00Z-
dc.date.available2017-04-19T09:22:00Z-
dc.date.issued2011-
dc.identifier.issn0014-5793-
dc.identifier.uri10.1016/j.febslet.2011.01.029ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10004-
dc.description.abstractHeat 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 Hsp331-235 (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 Hsp331-235, suggesting that a Hsp33 monomer is sufficient to interact with slowly unfolded substrate.-
dc.publisherWiley-
dc.titleCrystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity-
dc.title.alternativeCrystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity-
dc.typeArticle-
dc.citation.titleFEBS Letters-
dc.citation.number4-
dc.citation.endPage670-
dc.citation.startPage664-
dc.citation.volume585-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.affiliatedAuthorDae Gwin Jeong-
dc.contributor.affiliatedAuthorHye-Seon Lee-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorBo Yeon Kim-
dc.contributor.affiliatedAuthorSeung Jun Kim-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName정대균-
dc.contributor.alternativeName우주랑-
dc.contributor.alternativeName이혜선-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName김보연-
dc.contributor.alternativeNameErikson-
dc.contributor.alternativeName류성언-
dc.contributor.alternativeName김승준-
dc.identifier.bibliographicCitationFEBS Letters, vol. 585, no. 4, pp. 664-670-
dc.identifier.doi10.1016/j.febslet.2011.01.029-
dc.subject.keywordChaperone-
dc.subject.keywordDomain-swapping-
dc.subject.keywordHeat shock protein 33 (Hsp33)-
dc.subject.keywordRedox-sensitive-
dc.subject.localchaperone-
dc.subject.localChaperone-
dc.subject.localdomain swapping-
dc.subject.localDomain swapping-
dc.subject.localDomain-swapping-
dc.subject.localheat shock protein 33 (HSP 33)-
dc.subject.localHeat shock protein 33 (Hsp33)-
dc.subject.localRedox-sensitive-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
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