1zud

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(New page: 200px<br /><applet load="1zud" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zud, resolution 1.98&Aring;" /> '''Structure of ThiS-Th...)
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[[Image:1zud.gif|left|200px]]<br /><applet load="1zud" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zud.gif|left|200px]]<br /><applet load="1zud" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zud, resolution 1.98&Aring;" />
caption="1zud, resolution 1.98&Aring;" />
'''Structure of ThiS-ThiF protein complex'''<br />
'''Structure of ThiS-ThiF protein complex'''<br />
==Overview==
==Overview==
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We have determined the crystal structure of the Escherichia coli ThiS-ThiF, protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins, involved in the synthesis of the thiazole moiety of thiamin. ThiF, catalyzes the adenylation of the carboxy terminus of ThiS and the, subsequent displacement of AMP catalyzed by ThiI-persulfide to give a, ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur, donor for thiazole formation. ThiS is a small 7.2 kDa protein that, structurally resembles ubiquitin and the molybdopterin biosynthetic, protein MoaD. ThiF is a 27 kDa protein with distinct sequence and, structural similarity to the ubiquitin activating enzyme E1 and the, molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies, the mechanism of the sulfur transfer chemistry involved in thiazole, biosynthesis.
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We have determined the crystal structure of the Escherichia coli ThiS-ThiF protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins involved in the synthesis of the thiazole moiety of thiamin. ThiF catalyzes the adenylation of the carboxy terminus of ThiS and the subsequent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur donor for thiazole formation. ThiS is a small 7.2 kDa protein that structurally resembles ubiquitin and the molybdopterin biosynthetic protein MoaD. ThiF is a 27 kDa protein with distinct sequence and structural similarity to the ubiquitin activating enzyme E1 and the molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies the mechanism of the sulfur transfer chemistry involved in thiazole biosynthesis.
==About this Structure==
==About this Structure==
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1ZUD 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 ZN, CA and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZUD OCA].
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1ZUD 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=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUD OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Ealick, S.E.]]
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[[Category: Ealick, S E.]]
[[Category: Lehmann, C.]]
[[Category: Lehmann, C.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: this]]
[[Category: this]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:39:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:08 2008''

Revision as of 14:19, 21 February 2008

Image:1zud.gif

1zud, resolution 1.98Å

Drag the structure with the mouse to rotate

Structure of ThiS-ThiF protein complex

Overview

We have determined the crystal structure of the Escherichia coli ThiS-ThiF protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins involved in the synthesis of the thiazole moiety of thiamin. ThiF catalyzes the adenylation of the carboxy terminus of ThiS and the subsequent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur donor for thiazole formation. ThiS is a small 7.2 kDa protein that structurally resembles ubiquitin and the molybdopterin biosynthetic protein MoaD. ThiF is a 27 kDa protein with distinct sequence and structural similarity to the ubiquitin activating enzyme E1 and the molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies the mechanism of the sulfur transfer chemistry involved in thiazole biosynthesis.

About this Structure

1ZUD is a Protein complex structure of sequences from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis., Lehmann C, Begley TP, Ealick SE, Biochemistry. 2006 Jan 10;45(1):11-9. PMID:16388576

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