1t12
From Proteopedia
(New page: 200px<br /><applet load="1t12" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t12" /> '''Solution Structure of a new LTP1'''<br /> =...) |
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| - | [[Image:1t12.gif|left|200px]]<br /><applet load="1t12" size=" | + | [[Image:1t12.gif|left|200px]]<br /><applet load="1t12" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t12" /> | caption="1t12" /> | ||
'''Solution Structure of a new LTP1'''<br /> | '''Solution Structure of a new LTP1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Plant lipid transfer proteins are small soluble extracellular proteins | + | Plant lipid transfer proteins are small soluble extracellular proteins that are able to bind and transfer a variety of lipids in vitro. Recently, it has been proposed that lipid transfer proteins may play a key role in plant defence mechanisms, especially during the induction of systemic acquired resistance. However, very little is known about the proteins expressed in developing plants and tissues, since almost all the biophysical and structural data available to date on lipid transfer proteins originate from proteins present in storage tissues of monocot cereal seeds. In this paper, we report the structural and functional characteristics of a lipid transfer protein (named LTP1_1) constitutively expressed in young aerial organs of Nicotiana tabacum (common tobacco). The unlabelled and uniformly labelled proteins were produced in the yeast Pichia pastoris, and we determined the three-dimensional (3D) structure of LTP1_1 using nuclear magnetic resonance (NMR) spectroscopy and molecular modeling techniques. The global fold of LTP1_1 is very close to the previously published structures of LTP1 extracted from cereal seeds, including an internal cavity. However, the chemical shift variations of several NMR signals upon lipid binding show that tobacco LTP1_1 is able to bind only one LysoMyristoylPhosphatidylCholine (LMPC), while wheat and maize LTPs can bind either one or two. Titration experiments using intrinsic tyrosine fluorescence confirm this result not only with LMPC but also with two fatty acids. These differences can be explained by the presence in tobacco LTP1_1 of a hydrophobic cluster closing the second possible access to the protein cavity. This result suggests that LTP1 lipid binding properties could be modulated by subtle changes in a conserved global structure. The biological significance of this finding is discussed in the light of the signalling properties of the tobacco LTP1_1-jasmonate complex described elsewhere. |
==About this Structure== | ==About this Structure== | ||
| - | 1T12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http:// | + | 1T12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T12 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Landon, C.]] | [[Category: Landon, C.]] | ||
[[Category: Ponchet, M.]] | [[Category: Ponchet, M.]] | ||
| - | [[Category: Silva, P | + | [[Category: Silva, P da.]] |
[[Category: Vovelle, F.]] | [[Category: Vovelle, F.]] | ||
[[Category: cystein rich protein; lipid transfer protein]] | [[Category: cystein rich protein; lipid transfer protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:41 2008'' |
Revision as of 13:08, 21 February 2008
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Solution Structure of a new LTP1
Overview
Plant lipid transfer proteins are small soluble extracellular proteins that are able to bind and transfer a variety of lipids in vitro. Recently, it has been proposed that lipid transfer proteins may play a key role in plant defence mechanisms, especially during the induction of systemic acquired resistance. However, very little is known about the proteins expressed in developing plants and tissues, since almost all the biophysical and structural data available to date on lipid transfer proteins originate from proteins present in storage tissues of monocot cereal seeds. In this paper, we report the structural and functional characteristics of a lipid transfer protein (named LTP1_1) constitutively expressed in young aerial organs of Nicotiana tabacum (common tobacco). The unlabelled and uniformly labelled proteins were produced in the yeast Pichia pastoris, and we determined the three-dimensional (3D) structure of LTP1_1 using nuclear magnetic resonance (NMR) spectroscopy and molecular modeling techniques. The global fold of LTP1_1 is very close to the previously published structures of LTP1 extracted from cereal seeds, including an internal cavity. However, the chemical shift variations of several NMR signals upon lipid binding show that tobacco LTP1_1 is able to bind only one LysoMyristoylPhosphatidylCholine (LMPC), while wheat and maize LTPs can bind either one or two. Titration experiments using intrinsic tyrosine fluorescence confirm this result not only with LMPC but also with two fatty acids. These differences can be explained by the presence in tobacco LTP1_1 of a hydrophobic cluster closing the second possible access to the protein cavity. This result suggests that LTP1 lipid binding properties could be modulated by subtle changes in a conserved global structure. The biological significance of this finding is discussed in the light of the signalling properties of the tobacco LTP1_1-jasmonate complex described elsewhere.
About this Structure
1T12 is a Single protein structure of sequence from Nicotiana tabacum. Full crystallographic information is available from OCA.
Reference
Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features., Da Silva P, Landon C, Industri B, Marais A, Marion D, Ponchet M, Vovelle F, Proteins. 2005 May 1;59(2):356-67. PMID:15726627
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