1i7f
From Proteopedia
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| - | [[Image:1i7f.gif|left|200px]] | + | [[Image:1i7f.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY''' | + | {{Structure |
| + | |PDB= 1i7f |SIZE=350|CAPTION= <scene name='initialview01'>1i7f</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= HSP33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I7F is a [ | + | 1I7F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7F OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11323724 11323724] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: redox sensitive molecular chaperone]] | [[Category: redox sensitive molecular chaperone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:46:29 2008'' |
Revision as of 09:46, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | and | ||||||
| Gene: | HSP33 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE HSP33 DOMAIN WITH CONSTITUTIVE CHAPERONE ACTIVITY
Overview
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.
About this Structure
1I7F is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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