7bzx

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==DXPS==
==DXPS==
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<StructureSection load='7bzx' size='340' side='right'caption='[[7bzx]]' scene=''>
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<StructureSection load='7bzx' size='340' side='right'caption='[[7bzx]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BZX FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BZX FirstGlance]. <br>
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</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=7bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bzx OCA], [https://pdbe.org/7bzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bzx RCSB], [https://www.ebi.ac.uk/pdbsum/7bzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bzx ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bzx OCA], [https://pdbe.org/7bzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bzx RCSB], [https://www.ebi.ac.uk/pdbsum/7bzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bzx ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp-substrate complexes has been hampered by the transient and heterogeneous nature of their interactions, and the precise mechanisms underlying substrate recognition, promiscuity, and chaperone activity of sHsps remain unclear. Here we show the formation of a stable complex between Arabidopsis thaliana plastid sHsp, Hsp21, and its natural substrate 1-deoxy-D-xylulose 5-phosphate synthase (DXPS) under heat stress, and report cryo-electron microscopy structures of Hsp21, DXPS and Hsp21-DXPS complex at near-atomic resolution. Monomeric Hsp21 binds across the dimer interface of DXPS and engages in multivalent interactions by recognizing highly dynamic structural elements in DXPS. Hsp21 partly unfolds its central alpha-crystallin domain to facilitate binding of DXPS, which preserves a native-like structure. This mode of interaction suggests a mechanism of sHsps anti-aggregation activity towards a broad range of substrates.
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Structural basis of substrate recognition and thermal protection by a small heat shock protein.,Yu C, Leung SKP, Zhang W, Lai LTF, Chan YK, Wong MC, Benlekbir S, Cui Y, Jiang L, Lau WCY Nat Commun. 2021 May 21;12(1):3007. doi: 10.1038/s41467-021-23338-y. PMID:34021140<ref>PMID:34021140</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7bzx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lau WCY]]
[[Category: Lau WCY]]

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DXPS

PDB ID 7bzx

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