Semi-Empirical Structure Determination of Escherichia coli Hsp33 and Identification of Dynamic Regulatory Elements for the Activation Process
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- 作者：Yoo-Sup Lee1 ; 2 ; Jinhyuk Lee3 ; 4 ; 8 ; Kyoung-Seok Ryu5 ; Yuno Lee6 ; Tai-Geun Jung1 ; 9 ; Jeong-Hwa Jang1 ; Dae-Won Sim1 ; Eun-Hee Kim5 ; Min-Duk Seo2 ; 7 ; Keun Woo Lee6 ; Hyung-Sik Won1 ; wonhs@kku.ac.kr" class="auth_mail" title="E-mail the corresponding author
- 关键词：CRD ; C-terminal regulatory domain ; CS ; citrate synthase ; CSA ; conformational space annealing ; Hsp33 ; heat shock protein 33 ; HSQC ; heteronuclear single quantum coherence ; MALS ; multi-angle light scattering ; MLD ; middle linker domain ; NCD ; N-terminal core domain ; NOE ; nuclear Overhauser enhancement ; NOESY ; NOE spectroscopy ; TROSY ; transverse relaxation optimized spectroscopy
- 刊名：Journal of Molecular Biology
- 出版年：2015
- 出版时间：4 December 2015
- 年：2015
- 卷：427
- 期：24
- 页码：3850-3861
- 全文大小：1606 K
文摘
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The activation process of Hsp33 is accompanied by drastic alterations of conformation.
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Various conformations of wild-type and mutant Hsp33 were characterized by NMR.
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The N-terminal stretch (β1 and α1) was identified as a novel regulatory region.
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The regulatory module was dynamically organized in its inactive, reduced state.
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Molecular dynamics are structural determinants regulating molecular chaperones.