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-Structure paper
Title | A novel mechanism for small heat shock proteins to function as molecular chaperones. |
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Journal, issue, pages | Sci Rep, Vol. 5, Page 8811, Year 2015 |
Publish date | Mar 6, 2015 |
Authors | Kaiming Zhang / Anastasia N Ezemaduka / Zhao Wang / Hongli Hu / Xiaodong Shi / Chuang Liu / Xinping Lu / Xinmiao Fu / Zengyi Chang / Chang-Cheng Yin / |
PubMed Abstract | Small heat shock proteins (sHSPs) are molecular chaperones ubiquitously present in all forms of life, but their function mechanisms remain controversial. Here we show by cryo-electron microscopy and ...Small heat shock proteins (sHSPs) are molecular chaperones ubiquitously present in all forms of life, but their function mechanisms remain controversial. Here we show by cryo-electron microscopy and single particle 3D reconstruction that, at the low temperatures (4-25°C), CeHSP17 (a sHSP from Caenorhabditis elegans) exists as a 24-subunit spherical oligomer with tetrahedral symmetry. Our studies demonstrate that CeHSP17 forms large sheet-like super-molecular assemblies (SMAs) at the high temperatures (45-60°C), and such SMAs are apparently the form that exhibits chaperone-like activity. Our findings suggest a novel molecular mechanism for sHSPs to function as molecular chaperones. |
External links | Sci Rep / PubMed:25744691 / PubMed Central |
Methods | EM (single particle) |
Resolution | 14.5 Å |
Structure data | EMDB-2800: |
Source |
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