4eld

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Current revision (15:04, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eld]] is a 2 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=4ELD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ELD FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eld]] is a 2 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=4ELD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ELD 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=4eld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eld OCA], [https://pdbe.org/4eld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eld RCSB], [https://www.ebi.ac.uk/pdbsum/4eld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eld 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">X-ray diffraction, [[Resolution|Resolution]] 2.701&#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=4eld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eld OCA], [https://pdbe.org/4eld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eld RCSB], [https://www.ebi.ac.uk/pdbsum/4eld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eld ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HSPS_METJA HSPS_METJA]] Chaperone that confers thermal protection to other proteins.
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[https://www.uniprot.org/uniprot/HSPS_METJA HSPS_METJA] Chaperone that confers thermal protection to other proteins.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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How does the sequence of a single small heat shock protein (sHSP) assemble into oligomers of different sizes? To gain insight into the underlying structural mechanism, we determined the crystal structure of an engineered variant of Methanocaldococcus jannaschii Hsp16.5 wherein a 14 amino acid peptide from human heat shock protein 27 (Hsp27) was inserted at the junction of the N-terminal region and the alpha-crystallin domain. In response to this insertion, the oligomer shell expands from 24 to 48 subunits while maintaining octahedral symmetry. Oligomer rearrangement does not alter the fold of the conserved alpha-crystallin domain nor does it disturb the interface holding the dimeric building block together. Rather, the flexible C-terminal tail of Hsp16.5 changes its orientation relative to the alpha-crystallin domain which enables alternative packing of dimers. This change in orientation preserves a peptide-in-groove interaction of the C-terminal tail with an adjacent beta-sandwich, thereby holding the assembly together. The interior of the expanded oligomer, where substrates presumably bind, retains its predominantly nonpolar character relative to the outside surface. New large windows in the outer shell provide increased access to these substrate-binding regions, thus accounting for the higher affinity of this variant to substrates. Oligomer polydispersity regulates sHSPs chaperone activity in vitro and has been implicated in their physiological roles. The structural mechanism of Hsp16.5 oligomer flexibility revealed here, which is likely to be highly conserved across the sHSP superfamily, explains the relationship between oligomer expansion observed in disease-linked mutants and changes in chaperone activity.
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Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5.,McHaourab HS, Lin YL, Spiller BW Biochemistry. 2012 Jun 15. PMID:22670769<ref>PMID:22670769</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 4eld" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
 
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<references/>
 
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</StructureSection>
</StructureSection>

Current revision

Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5

PDB ID 4eld

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