1eej

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(New page: 200px<br /><applet load="1eej" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eej, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1eej.jpg|left|200px]]<br /><applet load="1eej" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1eej, resolution 1.90&Aring;" />
caption="1eej, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI'''<br />
'''CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI'''<br />
==Overview==
==Overview==
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DsbC is one of five Escherichia coli proteins required for disulfide bond, formation and is thought to function as a disulfide bond isomerase during, oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer, and has both protein disulfide isomerase and chaperone activity. We report, the 1.9 A resolution crystal structure of oxidized DsbC where both, Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of, separate thioredoxin-like domains joined via hinged linker helices to an, N-terminal dimerization domain. The hinges allow relative movement of the, active sites, and a broad uncharged cleft between them may be involved in, peptide binding and DsbC foldase activities.
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DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.
==About this Structure==
==About this Structure==
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1EEJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EEJ OCA].
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1EEJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEJ OCA].
==Reference==
==Reference==
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[[Category: Protein disulfide-isomerase]]
[[Category: Protein disulfide-isomerase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baker, E.N.]]
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[[Category: Baker, E N.]]
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[[Category: Haebel, P.W.]]
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[[Category: Haebel, P W.]]
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[[Category: McCarthy, A.A.]]
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[[Category: McCarthy, A A.]]
[[Category: Metcalf, P.]]
[[Category: Metcalf, P.]]
[[Category: Rybin, V.]]
[[Category: Rybin, V.]]
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[[Category: redox-active center]]
[[Category: redox-active center]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:56:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:57 2008''

Revision as of 10:27, 21 February 2008


1eej, resolution 1.90Å

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CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI

Overview

DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.

About this Structure

1EEJ is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Protein disulfide-isomerase, with EC number 5.3.4.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli., McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P, Nat Struct Biol. 2000 Mar;7(3):196-9. PMID:10700276

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