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| - | [[Image:2avx.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2avx| PDB=2avx | SCENE= }} | | {{STRUCTURE_2avx| PDB=2avx | SCENE= }} |
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| - | '''solution structure of E coli SdiA1-171'''
| + | ===solution structure of E coli SdiA1-171=== |
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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16307757}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16307757 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16307757}} |
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| | ==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]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Homoserine lactone]] | | [[Category: Homoserine lactone]] |
| | [[Category: Quorum sensing]] | | [[Category: Quorum sensing]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:32:14 2008'' | + | |
| | + | ''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
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
Page seeded by OCA on Mon Jul 28 05:58:26 2008