1y6d
From Proteopedia
(New page: 200px<br /><applet load="1y6d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y6d" /> '''Solution structure and dynamics of LuxU from...) |
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'''Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing'''<br /> | '''Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The marine bacterium Vibrio harveyi controls its bioluminescence by a | + | The marine bacterium Vibrio harveyi controls its bioluminescence by a process known as quorum sensing. In this process, autoinducer molecules are detected by membrane-bound sensor kinase/response regulator proteins (LuxN and LuxQ) that relay a signal via a series of protein phosphorylation reactions to another response regulator protein, LuxO. Phosphorylated LuxO indirectly represses the expression of the proteins responsible for bioluminescence. Integral to this quorum sensing process is the function of the phosphotransferase protein, LuxU. LuxU acts to shuttle the phosphate from the membrane-bound proteins, LuxN and LuxQ, to LuxO. LuxU is a 114 amino acid residue monomeric protein. Solution NMR was used to determine the three-dimensional structure of LuxU. LuxU contains a four-helix bundle topology with the active-site histidine residue (His58) located on alpha-helix C and exposed to solution. The active site represents a cluster of positively charged residues located on an otherwise hydrophobic protein face. NMR spin-relaxation experiments identify a collection of flexible residues localized on the same region of LuxU as His58. The studies described here represent the first structural characterization of an isolated, monomeric bacterial phosphotransferase protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http:// | + | 1Y6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio harveyi]] | [[Category: Vibrio harveyi]] | ||
| - | [[Category: Bassler, B | + | [[Category: Bassler, B L.]] |
[[Category: Cavanagh, J.]] | [[Category: Cavanagh, J.]] | ||
[[Category: Kojetin, D.]] | [[Category: Kojetin, D.]] | ||
| - | [[Category: Loria, J | + | [[Category: Loria, J P.]] |
| - | [[Category: Ulrich, D | + | [[Category: Ulrich, D L.]] |
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
[[Category: phosphorelay]] | [[Category: phosphorelay]] | ||
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[[Category: quorum sensing]] | [[Category: quorum sensing]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:09 2008'' |
Revision as of 14:02, 21 February 2008
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Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing
Overview
The marine bacterium Vibrio harveyi controls its bioluminescence by a process known as quorum sensing. In this process, autoinducer molecules are detected by membrane-bound sensor kinase/response regulator proteins (LuxN and LuxQ) that relay a signal via a series of protein phosphorylation reactions to another response regulator protein, LuxO. Phosphorylated LuxO indirectly represses the expression of the proteins responsible for bioluminescence. Integral to this quorum sensing process is the function of the phosphotransferase protein, LuxU. LuxU acts to shuttle the phosphate from the membrane-bound proteins, LuxN and LuxQ, to LuxO. LuxU is a 114 amino acid residue monomeric protein. Solution NMR was used to determine the three-dimensional structure of LuxU. LuxU contains a four-helix bundle topology with the active-site histidine residue (His58) located on alpha-helix C and exposed to solution. The active site represents a cluster of positively charged residues located on an otherwise hydrophobic protein face. NMR spin-relaxation experiments identify a collection of flexible residues localized on the same region of LuxU as His58. The studies described here represent the first structural characterization of an isolated, monomeric bacterial phosphotransferase protein.
About this Structure
1Y6D is a Single protein structure of sequence from Vibrio harveyi. Full crystallographic information is available from OCA.
Reference
Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing., Ulrich DL, Kojetin D, Bassler BL, Cavanagh J, Loria JP, J Mol Biol. 2005 Mar 25;347(2):297-307. PMID:15740742
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