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==Small-heat shock protein from Methanocaldococcus jannaschii, Hsp16.5==
<StructureSection load='8wp9' size='340' side='right'caption='[[8wp9]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8wp9]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WP9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8wp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wp9 OCA], [https://pdbe.org/8wp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wp9 RCSB], [https://www.ebi.ac.uk/pdbsum/8wp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wp9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSPS_METJA HSPS_METJA] Chaperone that confers thermal protection to other proteins.
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== Publication Abstract from PubMed ==
The 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<ref>PMID:38103675</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8wp9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Kim KK]]
[[Category: Kim T]]
[[Category: Lee J]]
[[Category: Ryu B]]