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1i7f

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Revision as of 07:36, 7 April 2021

CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY

Structural highlights

1i7f is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HSLO_ECOLI] Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.[HAMAP-Rule:MF_00117]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Heat shock protein 33 (Hsp33) inhibits aggregation of partially denatured proteins during oxidative stress. The chaperone activity of Hsp33 is unique among heat shock proteins because the activity is reversibly regulated by cellular redox status. We report here the crystal structure of the N-terminal region of Hsp33 fragments with constitutive chaperone activity. The structure reveals that the N-terminal portion of Hsp33 forms a tightly associated dimer formed by a domain crossover. A concave groove on the dimeric surface contains an elongated hydrophobic patch that could potentially bind denatured protein substrates. The termini of the subunits are located near the hydrophobic patch, indicating that the cleaved C-terminal domain may shield the hydrophobic patch in an inactive state. Two of the four conserved zinc-coordinating cysteines are in the end of the N-terminal domain, and the other two are in the cleaved C-terminal domain. The structural information and subsequent biochemical characterizations suggest that the redox switch of Hsp33 occurs by a reversible dissociation of the C-terminal regulatory domain through oxidation of zinc-coordinating cysteines and zinc release.

Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity.,Kim SJ, Jeong DG, Chi SW, Lee JS, Ryu SE Nat Struct Biol. 2001 May;8(5):459-66. PMID:11323724^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kim SJ, Jeong DG, Chi SW, Lee JS, Ryu SE. Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity. Nat Struct Biol. 2001 May;8(5):459-66. PMID:11323724 doi:10.1038/87639

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i7f"

@@ Line 3: / Line 3: @@
 <StructureSection load='1i7f' size='340' side='right'caption='[[1i7f]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1i7f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I7F FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1i7f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I7F FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7f OCA], [http://pdbe.org/1i7f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i7f RCSB], [http://www.ebi.ac.uk/pdbsum/1i7f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7f ProSAT]</span></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=1i7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7f OCA], [https://pdbe.org/1i7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i7f RCSB], [https://www.ebi.ac.uk/pdbsum/1i7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7f ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HSLO_ECOLI HSLO_ECOLI]] Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.[HAMAP-Rule:MF_00117]
+[[https://www.uniprot.org/uniprot/HSLO_ECOLI HSLO_ECOLI]] Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.[HAMAP-Rule:MF_00117]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Heat Shock Proteins|Heat Shock Proteins]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>

1i7f

From Proteopedia

Revision as of 07:36, 7 April 2021

CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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