1z5y

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(New page: 200px<br /><applet load="1z5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z5y, resolution 1.94&Aring;" /> '''Crystal Structure Of...)
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'''Crystal Structure Of The Disulfide-Linked Complex Between The N-Terminal Domain Of The Electron Transfer Catalyst DsbD and The Cytochrome c Biogenesis Protein CcmG'''<br />
'''Crystal Structure Of The Disulfide-Linked Complex Between The N-Terminal Domain Of The Electron Transfer Catalyst DsbD and The Cytochrome c Biogenesis Protein CcmG'''<br />
==Overview==
==Overview==
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DsbD from Escherichia coli transports two electrons from cytoplasmic, thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG., DsbD consists of an N-terminal periplasmic domain (nDsbD), a C-terminal, periplasmic domain, and a central transmembrane domain. Each domain, possesses two cysteines required for electron transport. Herein, we, demonstrate fast (3.9 x 10(5) M(-1)s(-1)) and direct disulfide exchange, between nDsbD and CcmG, a highly specific disulfide reductase essential, for cytochrome c maturation. We determined the crystal structure of the, disulfide-linked complex between nDsbD and the soluble part of CcmG at, 1.94 A resolution. In contrast to the other two known complexes of nDsbD, with target proteins, the N-terminal segment of nDsbD contributes to, specific recognition of CcmG. This and other features, like the, possibility of using an additional interaction surface, constitute the, structural basis for the adaptability of nDsbD to different protein, substrates.
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DsbD from Escherichia coli transports two electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG. DsbD consists of an N-terminal periplasmic domain (nDsbD), a C-terminal periplasmic domain, and a central transmembrane domain. Each domain possesses two cysteines required for electron transport. Herein, we demonstrate fast (3.9 x 10(5) M(-1)s(-1)) and direct disulfide exchange between nDsbD and CcmG, a highly specific disulfide reductase essential for cytochrome c maturation. We determined the crystal structure of the disulfide-linked complex between nDsbD and the soluble part of CcmG at 1.94 A resolution. In contrast to the other two known complexes of nDsbD with target proteins, the N-terminal segment of nDsbD contributes to specific recognition of CcmG. This and other features, like the possibility of using an additional interaction surface, constitute the structural basis for the adaptability of nDsbD to different protein substrates.
==About this Structure==
==About this Structure==
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1Z5Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-disulfide_reductase Protein-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.8 1.8.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z5Y OCA].
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1Z5Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-disulfide_reductase Protein-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.8 1.8.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5Y OCA].
==Reference==
==Reference==
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[[Category: Glockshuber, R.]]
[[Category: Glockshuber, R.]]
[[Category: Grauschopf, U.]]
[[Category: Grauschopf, U.]]
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[[Category: Gruetter, M.G.]]
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[[Category: Gruetter, M G.]]
[[Category: Rozhkova, A.]]
[[Category: Rozhkova, A.]]
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[[Category: Stirnimann, C.U.]]
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[[Category: Stirnimann, C U.]]
[[Category: CL]]
[[Category: CL]]
[[Category: EDO]]
[[Category: EDO]]
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[[Category: thioredoxin-like]]
[[Category: thioredoxin-like]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:15:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:21 2008''

Revision as of 14:12, 21 February 2008


1z5y, resolution 1.94Å

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Crystal Structure Of The Disulfide-Linked Complex Between The N-Terminal Domain Of The Electron Transfer Catalyst DsbD and The Cytochrome c Biogenesis Protein CcmG

Overview

DsbD from Escherichia coli transports two electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG. DsbD consists of an N-terminal periplasmic domain (nDsbD), a C-terminal periplasmic domain, and a central transmembrane domain. Each domain possesses two cysteines required for electron transport. Herein, we demonstrate fast (3.9 x 10(5) M(-1)s(-1)) and direct disulfide exchange between nDsbD and CcmG, a highly specific disulfide reductase essential for cytochrome c maturation. We determined the crystal structure of the disulfide-linked complex between nDsbD and the soluble part of CcmG at 1.94 A resolution. In contrast to the other two known complexes of nDsbD with target proteins, the N-terminal segment of nDsbD contributes to specific recognition of CcmG. This and other features, like the possibility of using an additional interaction surface, constitute the structural basis for the adaptability of nDsbD to different protein substrates.

About this Structure

1Z5Y is a Protein complex structure of sequences from Escherichia coli with and as ligands. Active as Protein-disulfide reductase, with EC number 1.8.1.8 Full crystallographic information is available from OCA.

Reference

Structural basis and kinetics of DsbD-dependent cytochrome c maturation., Stirnimann CU, Rozhkova A, Grauschopf U, Grutter MG, Glockshuber R, Capitani G, Structure. 2005 Jul;13(7):985-93. PMID:16004871

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