1jzo: Difference between revisions
New page: left|200px<br /><applet load="1jzo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jzo, resolution 1.92Å" /> '''DsbC C101S'''<br /> ... |
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[[Image:1jzo.gif|left|200px]]<br /><applet load="1jzo" size=" | [[Image:1jzo.gif|left|200px]]<br /><applet load="1jzo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jzo, resolution 1.92Å" /> | caption="1jzo, resolution 1.92Å" /> | ||
'''DsbC C101S'''<br /> | '''DsbC C101S'''<br /> | ||
==Overview== | ==Overview== | ||
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect | The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm. | ||
==About this Structure== | ==About this Structure== | ||
1JZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1JZO is a [http://en.wikipedia.org/wiki/Single_protein 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=1JZO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Beckwith, J.]] | [[Category: Beckwith, J.]] | ||
[[Category: Goldstone, D.]] | [[Category: Goldstone, D.]] | ||
[[Category: Haebel, P | [[Category: Haebel, P W.]] | ||
[[Category: Katzen, F.]] | [[Category: Katzen, F.]] | ||
[[Category: Metcalf, P.]] | [[Category: Metcalf, P.]] | ||
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[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:29 2008'' | ||
Revision as of 14:28, 21 February 2008
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DsbC C101S
OverviewOverview
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.
About this StructureAbout this Structure
1JZO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex., Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P, EMBO J. 2002 Sep 16;21(18):4774-84. PMID:12234918
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