View source for 7bzy


==Hsp21-DXPS==
<StructureSection load='7bzy' size='340' side='right'caption='[[7bzy]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bzy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BZY 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]] 3.7&#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=7bzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bzy OCA], [https://pdbe.org/7bzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bzy RCSB], [https://www.ebi.ac.uk/pdbsum/7bzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bzy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DXS_ARATH DXS_ARATH] Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). Is a limiting enzyme for plastidic isoprenoid biosynthesis and essential for chloroplast development.<ref>PMID:10982425</ref> <ref>PMID:11264287</ref> <ref>PMID:8653115</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bzy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Lau WCY]]