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1tuk
From Proteopedia
(New page: 200px<br /><applet load="1tuk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tuk, resolution 1.12Å" /> '''Crystal stucture of ...) |
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| - | [[Image:1tuk.gif|left|200px]]<br /><applet load="1tuk" size=" | + | [[Image:1tuk.gif|left|200px]]<br /><applet load="1tuk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tuk, resolution 1.12Å" /> | caption="1tuk, resolution 1.12Å" /> | ||
'''Crystal stucture of liganted type 2 non specific lipid transfer protein from wheat'''<br /> | '''Crystal stucture of liganted type 2 non specific lipid transfer protein from wheat'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In plants, a family of ubiquitous proteins named non-specific | + | In plants, a family of ubiquitous proteins named non-specific lipid-transfer proteins (ns-LTPs) facilitates the transfer of fatty acids, phospholipids and steroids between membranes. Recent data suggest that these secreted proteins play a key role in the formation of cuticular wax layers and in defence mechanisms against pathogens. In this study, X-ray crystallography has been used to examine the structural details of the interaction between a wheat type 2 ns-LTP and a lipid, L-alpha-palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 A resolution by direct methods. The typical alpha-helical bundle fold of this protein is maintained by four disulfide bridges and delineates two hydrophobic cavities. The inner surface of the main cavity is lined by non-polar residues that provide a hydrophobic environment for the palmitoyl moiety of the lipid. The head-group region of this lipid protrudes from the surface and makes several polar interactions with a conserved patch of basic residues at the entrance of the pocket. The alkyl chain of a second lipid is bound within an adjacent smaller cavity. The structure shows that binding of the lipid tails to the protein involves extensive hydrophobic interactions. |
==About this Structure== | ==About this Structure== | ||
| - | 1TUK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with IOD and PGM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1TUK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with <scene name='pdbligand=IOD:'>IOD</scene> and <scene name='pdbligand=PGM:'>PGM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Triticum aestivum]] | [[Category: Triticum aestivum]] | ||
[[Category: Dumas, C.]] | [[Category: Dumas, C.]] | ||
| - | [[Category: Gautier, M | + | [[Category: Gautier, M F.]] |
[[Category: Hoh, F.]] | [[Category: Hoh, F.]] | ||
| - | [[Category: Lamotte, F | + | [[Category: Lamotte, F De.]] |
| - | [[Category: Pons, J | + | [[Category: Pons, J L.]] |
[[Category: IOD]] | [[Category: IOD]] | ||
[[Category: PGM]] | [[Category: PGM]] | ||
| Line 23: | Line 23: | ||
[[Category: ns-ltp2]] | [[Category: ns-ltp2]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:34 2008'' |
Revision as of 13:17, 21 February 2008
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Crystal stucture of liganted type 2 non specific lipid transfer protein from wheat
Overview
In plants, a family of ubiquitous proteins named non-specific lipid-transfer proteins (ns-LTPs) facilitates the transfer of fatty acids, phospholipids and steroids between membranes. Recent data suggest that these secreted proteins play a key role in the formation of cuticular wax layers and in defence mechanisms against pathogens. In this study, X-ray crystallography has been used to examine the structural details of the interaction between a wheat type 2 ns-LTP and a lipid, L-alpha-palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 A resolution by direct methods. The typical alpha-helical bundle fold of this protein is maintained by four disulfide bridges and delineates two hydrophobic cavities. The inner surface of the main cavity is lined by non-polar residues that provide a hydrophobic environment for the palmitoyl moiety of the lipid. The head-group region of this lipid protrudes from the surface and makes several polar interactions with a conserved patch of basic residues at the entrance of the pocket. The alkyl chain of a second lipid is bound within an adjacent smaller cavity. The structure shows that binding of the lipid tails to the protein involves extensive hydrophobic interactions.
About this Structure
1TUK is a Single protein structure of sequence from Triticum aestivum with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding., Hoh F, Pons JL, Gautier MF, de Lamotte F, Dumas C, Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):397-406. Epub 2005, Mar 24. PMID:15805594
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