8wp9 | pdb_00008wp9
Small-heat shock protein from Methanocaldococcus jannaschii, Hsp16.5
Structural highlights
FunctionHSPS_METJA Chaperone that confers thermal protection to other proteins. Publication Abstract from PubMedThe small heat-shock protein (sHSP) from the archaea Methanocaldococcus jannaschii, MjsHSP16.5, functions as a broad substrate ATP-independent holding chaperone protecting misfolded proteins from aggregation under stress conditions. This protein is the first sHSP characterized by X-ray crystallography, thereby contributing significantly to our understanding of sHSPs. However, despite numerous studies assessing its functions and structures, the precise arrangement of the N-terminal domains (NTDs) within this sHSP cage remains elusive. Here we present the cryo-electron microscopy (cryo-EM) structure of MjsHSP16.5 at 2.49-A resolution. The subunits of MjsHSP16.5 in the cryo-EM structure exhibit lesser compaction compared to their counterparts in the crystal structure. This structural feature holds particular significance in relation to the biophysical properties of MjsHSP16.5, suggesting a close resemblance to this sHSP native state. Additionally, our cryo-EM structure unveils the density of residues 24-33 within the NTD of MjsHSP16.5, a feature that typically remains invisible in the majority of its crystal structures. Notably, these residues show a propensity to adopt a beta-strand conformation and engage in antiparallel interactions with strand beta1, both intra- and inter-subunit modes. These structural insights are corroborated by structural predictions, disulfide bond cross-linking studies of Cys-substitution mutants, and protein disaggregation assays. A comprehensive understanding of the structural features of MjsHSP16.5 expectedly holds the potential to inspire a wide range of interdisciplinary applications, owing to the renowned versatility of this sHSP as a nanoscale protein platform. Cryo-EM structure of a 16.5-kDa small heat-shock protein from Methanocaldococcus jannaschii.,Lee J, Ryu B, Kim T, Kim KK Int J Biol Macromol. 2023 Dec 15;258(Pt 1):128763. doi: , 10.1016/j.ijbiomac.2023.128763. PMID:38103675[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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