1t3b

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(New page: 200px<br /><applet load="1t3b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t3b, resolution 2.5&Aring;" /> '''X-ray Structure of Ds...)
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[[Image:1t3b.gif|left|200px]]<br /><applet load="1t3b" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t3b, resolution 2.5&Aring;" />
caption="1t3b, resolution 2.5&Aring;" />
'''X-ray Structure of DsbC from Haemophilus influenzae'''<br />
'''X-ray Structure of DsbC from Haemophilus influenzae'''<br />
==Overview==
==Overview==
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Bacterial DsbC proteins are involved in rearranging or reducing mismatched, disulfide bonds folding within the periplasm. The X-ray structure of the, enzyme from Haemophilus influenzae has been solved and compared with the, known structure of the Escherichia coli protein. The proteins act as, V-shaped dimers with a large cleft to accommodate substrate proteins. The, dimers are anchored by a small N-terminal domain, but have a flexible, linker region which allows the larger C-terminal domain, with its reactive, sulfhydryls, to clamp down on substrates. The overall folds are very, similar, but the comparison shows a wider range of hinge motions than, previously thought. The crystal packing of the H. influenzae protein, allows the movement of the N-terminal domain with respect to the, C-terminal domain through motions in the flexible hinge, generating high, thermal parameters and unusually high anisotropy in the crystallographic, data.
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Bacterial DsbC proteins are involved in rearranging or reducing mismatched disulfide bonds folding within the periplasm. The X-ray structure of the enzyme from Haemophilus influenzae has been solved and compared with the known structure of the Escherichia coli protein. The proteins act as V-shaped dimers with a large cleft to accommodate substrate proteins. The dimers are anchored by a small N-terminal domain, but have a flexible linker region which allows the larger C-terminal domain, with its reactive sulfhydryls, to clamp down on substrates. The overall folds are very similar, but the comparison shows a wider range of hinge motions than previously thought. The crystal packing of the H. influenzae protein allows the movement of the N-terminal domain with respect to the C-terminal domain through motions in the flexible hinge, generating high thermal parameters and unusually high anisotropy in the crystallographic data.
==About this Structure==
==About this Structure==
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1T3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. 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=1T3B OCA].
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1T3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. 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=1T3B OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Georgiou, G.]]
[[Category: Georgiou, G.]]
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[[Category: Monzingo, A.F.]]
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[[Category: Monzingo, A F.]]
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[[Category: Robertus, J.D.]]
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[[Category: Robertus, J D.]]
[[Category: Segatori, L.]]
[[Category: Segatori, L.]]
[[Category: Zhang, M.]]
[[Category: Zhang, M.]]
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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 Wed Nov 21 02:57:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:27 2008''

Revision as of 13:09, 21 February 2008


1t3b, resolution 2.5Å

Drag the structure with the mouse to rotate

X-ray Structure of DsbC from Haemophilus influenzae

Overview

Bacterial DsbC proteins are involved in rearranging or reducing mismatched disulfide bonds folding within the periplasm. The X-ray structure of the enzyme from Haemophilus influenzae has been solved and compared with the known structure of the Escherichia coli protein. The proteins act as V-shaped dimers with a large cleft to accommodate substrate proteins. The dimers are anchored by a small N-terminal domain, but have a flexible linker region which allows the larger C-terminal domain, with its reactive sulfhydryls, to clamp down on substrates. The overall folds are very similar, but the comparison shows a wider range of hinge motions than previously thought. The crystal packing of the H. influenzae protein allows the movement of the N-terminal domain with respect to the C-terminal domain through motions in the flexible hinge, generating high thermal parameters and unusually high anisotropy in the crystallographic data.

About this Structure

1T3B is a Single protein structure of sequence from Haemophilus influenzae. Active as Protein disulfide-isomerase, with EC number 5.3.4.1 Full crystallographic information is available from OCA.

Reference

Structure of DsbC from Haemophilus influenzae., Zhang M, Monzingo AF, Segatori L, Georgiou G, Robertus JD, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1512-8. Epub 2004, Aug 26. PMID:15333920

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