2avx: Difference between revisions

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[[Image:2avx.gif|left|200px]]
{{Seed}}
[[Image:2avx.png|left|200px]]


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{{STRUCTURE_2avx|  PDB=2avx  |  SCENE=  }}  
{{STRUCTURE_2avx|  PDB=2avx  |  SCENE=  }}  


'''solution structure of E coli SdiA1-171'''
===solution structure of E coli SdiA1-171===




==Overview==
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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.
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{{ABSTRACT_PUBMED_16307757}}


==About this Structure==
==About this Structure==
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].  
2AVX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AVX OCA].  


==Reference==
==Reference==
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[[Category: Homoserine lactone]]
[[Category: Homoserine lactone]]
[[Category: Quorum sensing]]
[[Category: Quorum sensing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:58:26 2008''

Revision as of 02:58, 28 July 2008

File:2avx.png

Template:STRUCTURE 2avx

solution structure of E coli SdiA1-171

Template:ABSTRACT PUBMED 16307757

About this Structure

2AVX is a Single protein structure of sequence from Escherichia coli. Full experimental 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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