2avx: Difference between revisions
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[[Image:2avx.gif|left|200px]]< | [[Image:2avx.gif|left|200px]] | ||
'''solution structure of E coli SdiA1-171''' | {{Structure | ||
|PDB= 2avx |SIZE=350|CAPTION= <scene name='initialview01'>2avx</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HTF:N-(2-OXOTETRAHYDROFURAN-3-YL)OCTANAMIDE'>HTF</scene> | |||
|ACTIVITY= | |||
|GENE= sdiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''solution structure of E coli SdiA1-171''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2AVX is a [ | 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== | ||
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:// | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''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
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| Ligands: | HTF | ||||||||||||
| 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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