2avu

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(New page: 200px<br /><applet load="2avu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2avu, resolution 3.00&Aring;" /> '''Structure of the Esc...)
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[[Image:2avu.gif|left|200px]]<br /><applet load="2avu" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2avu.gif|left|200px]]<br /><applet load="2avu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2avu, resolution 3.00&Aring;" />
caption="2avu, resolution 3.00&Aring;" />
'''Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription'''<br />
'''Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription'''<br />
==Overview==
==Overview==
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The hetero-oligomeric complex of the FlhD and FlhC proteins (FlhDC), regulates transcription from several flagellar and non-flagellar operons, in bacteria. The crystallographic structure of the Escherichia coli FlhDC, complex has been solved to 3.0 A resolution, revealing a hexameric, FlhD4FlhC2 assembly. In the complex, each FlhC protomer binds an FlhD2, dimer; the conformation of the dimer in the complex differs significantly, from its conformation in the absence of FlhC. FlhC has a novel tertiary, fold that includes a heretofore unrecognized zinc-binding site in which, the ion is ligated by four cysteine residues. Gel shift experiments show, that binding of the FlhDC complex to a cognate promoter bends the DNA by, approximately 111 degrees . The structure of the FlhDC complex is, compatible with models in which a fragment of operator DNA, at least 48, base-pairs in length, wraps around the complex and bends significantly, when binding.
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The hetero-oligomeric complex of the FlhD and FlhC proteins (FlhDC) regulates transcription from several flagellar and non-flagellar operons in bacteria. The crystallographic structure of the Escherichia coli FlhDC complex has been solved to 3.0 A resolution, revealing a hexameric FlhD4FlhC2 assembly. In the complex, each FlhC protomer binds an FlhD2 dimer; the conformation of the dimer in the complex differs significantly from its conformation in the absence of FlhC. FlhC has a novel tertiary fold that includes a heretofore unrecognized zinc-binding site in which the ion is ligated by four cysteine residues. Gel shift experiments show that binding of the FlhDC complex to a cognate promoter bends the DNA by approximately 111 degrees . The structure of the FlhDC complex is compatible with models in which a fragment of operator DNA, at least 48 base-pairs in length, wraps around the complex and bends significantly when binding.
==About this Structure==
==About this Structure==
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2AVU 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AVU OCA].
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2AVU 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AVU OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Fleming, R.T.]]
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[[Category: Fleming, R T.]]
[[Category: Matsumura, P.]]
[[Category: Matsumura, P.]]
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[[Category: McKay, D.B.]]
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[[Category: McKay, D B.]]
[[Category: Wang, S.]]
[[Category: Wang, S.]]
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[[Category: Westbrook, E.M.]]
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[[Category: Westbrook, E M.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: c4-type zinc finger]]
[[Category: c4-type zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:23:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:29 2008''

Revision as of 14:31, 21 February 2008


2avu, resolution 3.00Å

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Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription

Overview

The hetero-oligomeric complex of the FlhD and FlhC proteins (FlhDC) regulates transcription from several flagellar and non-flagellar operons in bacteria. The crystallographic structure of the Escherichia coli FlhDC complex has been solved to 3.0 A resolution, revealing a hexameric FlhD4FlhC2 assembly. In the complex, each FlhC protomer binds an FlhD2 dimer; the conformation of the dimer in the complex differs significantly from its conformation in the absence of FlhC. FlhC has a novel tertiary fold that includes a heretofore unrecognized zinc-binding site in which the ion is ligated by four cysteine residues. Gel shift experiments show that binding of the FlhDC complex to a cognate promoter bends the DNA by approximately 111 degrees . The structure of the FlhDC complex is compatible with models in which a fragment of operator DNA, at least 48 base-pairs in length, wraps around the complex and bends significantly when binding.

About this Structure

2AVU is a Protein complex structure of sequences from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription., Wang S, Fleming RT, Westbrook EM, Matsumura P, McKay DB, J Mol Biol. 2006 Jan 27;355(4):798-808. Epub 2005 Nov 22. PMID:16337229

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