1n89: Difference between revisions

Revision as of 11:04, 29 July 2008

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File:1n89.png

Template:STRUCTURE 1n89

Solution structure of a liganded type 2 wheat non-specific Lipid Transfer ProteinSolution structure of a liganded type 2 wheat non-specific Lipid Transfer Protein

Template:ABSTRACT PUBMED 12525478

About this StructureAbout this Structure

1N89 is a Single protein structure of sequence from Triticum turgidum subsp. durum. Full experimental information is available from OCA.

ReferenceReference

Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein., Pons JL, de Lamotte F, Gautier MF, Delsuc MA, J Biol Chem. 2003 Apr 18;278(16):14249-56. Epub 2003 Jan 13. PMID:12525478

Page seeded by OCA on Tue Jul 29 11:04:37 2008

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-[[Image:1n89.gif|left|200px]]
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 {{STRUCTURE_1n89|  PDB=1n89  |  SCENE=  }}
-'''Solution structure of a liganded type 2 wheat non-specific Lipid Transfer Protein'''
+===Solution structure of a liganded type 2 wheat non-specific Lipid Transfer Protein===
-==Overview==
+<!--
-The refined structure of a wheat type 2 nonspecific lipid transfer protein (ns-LTP2) liganded with l-alpha-palmitoylphosphatidylglycerol has been determined by NMR. The (15)N-labeled protein was produced in Pichia pastoris. Physicochemical conditions and ligandation were intensively screened to obtain the best NMR spectra quality. This ns-LTP2 is a 67-residue globular protein with a diameter of about 30 A. The structure is composed of five helices forming a right superhelix. The protein presents an inner cavity, which has been measured at 341 A(3). All of the helices display hydrophobic side chains oriented toward the cavity. The phospholipid is found in this cavity. Its fatty acid chain is completely inserted in the protein, the l-alpha-palmitoylphosphatidylglycerol glycerol moiety being located on a positively charged pocket on the surface of the protein. The superhelix structure of the protein is coiled around the fatty acid chain. The overall structure shows similarities with ns-LTP1. Nevertheless, large three-dimensional structural discrepancies are observed for the H3 and H4 alpha-helices, the C-terminal region, and the last turn of the H2 helix. The lipid is orthogonal to the orientation observed in ns-LTP1. The volume of the hydrophobic cavity appears to be in the same range as the one of ns-LTP1, despite the fact that ns-LTP2 is shorter by 24 residues.
+The line below this paragraph, {{ABSTRACT_PUBMED_12525478}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12525478 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12525478}}
 ==About this Structure==
-N89 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_turgidum_subsp._durum Triticum turgidum subsp. durum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N89 OCA].
+N89 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_turgidum_subsp._durum Triticum turgidum subsp. durum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N89 OCA].
 ==Reference==
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 [[Category: Pons, J L.]]
 [[Category: Lipid transfer protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:13:11 2008''
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