2avx

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[[Image:2avx.gif|left|200px]]<br /><applet load="2avx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2avx.gif|left|200px]]
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caption="2avx" />
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'''solution structure of E coli SdiA1-171'''<br />
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{{Structure
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|PDB= 2avx |SIZE=350|CAPTION= <scene name='initialview01'>2avx</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=HTF:N-(2-OXOTETRAHYDROFURAN-3-YL)OCTANAMIDE'>HTF</scene>
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|ACTIVITY=
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|GENE= sdiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''solution structure of E coli SdiA1-171'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AVX 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=HTF:'>HTF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AVX OCA].
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2AVX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AVX OCA].
==Reference==
==Reference==
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Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones., Yao Y, Martinez-Yamout MA, Dickerson TJ, Brogan AP, Wright PE, Dyson HJ, J Mol Biol. 2006 Jan 13;355(2):262-73. Epub 2005 Nov 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16307757 16307757]
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Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones., Yao Y, Martinez-Yamout MA, Dickerson TJ, Brogan AP, Wright PE, Dyson HJ, J Mol Biol. 2006 Jan 13;355(2):262-73. Epub 2005 Nov 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16307757 16307757]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: quorum sensing]]
[[Category: quorum sensing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:54:31 2008''

Revision as of 13:54, 20 March 2008


PDB ID 2avx

Drag the structure with the mouse to rotate
Ligands:
Gene: sdiA (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



solution structure of E coli SdiA1-171


Overview

The three-dimensional structure of a complex between the N-terminal domain of the quorum sensing protein SdiA of Escherichia coli and a candidate autoinducer N-octanoyl-L-homoserine lactone (C8-HSL) has been calculated in solution from NMR data. The SdiA-HSL system shows the "folding switch" behavior that has been seen for quorum-sensing factors produced by other bacterial species. In the presence of C8-HSL, a significant proportion of the SdiA protein is produced in a folded, soluble form in an E.coli expression system, whereas in the absence of acyl homoserine lactones, the protein is expressed into insoluble inclusion bodies. In the three-dimensional structure, the autoinducer molecule is sequestered in a deep pocket in the hydrophobic core, forming an integral part of the core packing of the folded SdiA. The NMR spectra of the complex show that the bound C8-HSL is conformationally heterogeneous, either due to motion within the pocket or to heterogeneity of the bound structure. The C8-HSL conformation is defined by NOEs to the protein only at the terminal methyl group of the octanoyl chain. Unlike other well-studied bacterial quorum sensing systems such as LuxR of Vibrio fischeri and TraR of Agrobacterium tumefaciens, there is no endogenous autoinducer for SdiA in E.coli: the E.coli genome does not contain a gene analogous to the LuxI and TraI autoinducer synthetases. We show that two other homoserine lactone derivatives are also capable of acting as a folding-switch autoinducers for SdiA. The observed structural heterogeneity of the bound C8-HSL in the complex, together with the variety of autoinducer-type molecules that can apparently act as folding switches in this system, are consistent with the postulated biological function of the SdiA protein as a detector of the presence of other species of bacteria.

About this Structure

2AVX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones., Yao Y, Martinez-Yamout MA, Dickerson TJ, Brogan AP, Wright PE, Dyson HJ, J Mol Biol. 2006 Jan 13;355(2):262-73. Epub 2005 Nov 8. PMID:16307757

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