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| | ==LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES== | | ==LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES== |
| - | <StructureSection load='1bv2' size='340' side='right'caption='[[1bv2]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''> | + | <StructureSection load='1bv2' size='340' side='right'caption='[[1bv2]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bv2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BV2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bv2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BV2 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bv2 OCA], [http://pdbe.org/1bv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bv2 RCSB], [http://www.ebi.ac.uk/pdbsum/1bv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bv2 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 14 models</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bv2 OCA], [https://pdbe.org/1bv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bv2 RCSB], [https://www.ebi.ac.uk/pdbsum/1bv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bv2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NLTP1_ORYSJ NLTP1_ORYSJ] Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/1bv2_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/1bv2_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryza sativa]] | | [[Category: Oryza sativa]] |
| - | [[Category: Lee, J Y]] | + | [[Category: Lee JY]] |
| - | [[Category: Poznanski, J]] | + | [[Category: Poznanski J]] |
| - | [[Category: Ptak, M]] | + | [[Category: Ptak M]] |
| - | [[Category: Sodano, P]] | + | [[Category: Sodano P]] |
| - | [[Category: Suh, S W]] | + | [[Category: Suh SW]] |
| - | [[Category: Vovelle, F]] | + | [[Category: Vovelle F]] |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Lipid transfer protein]]
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| - | [[Category: Lipid-binding protein]]
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| - | [[Category: Molecular modeling]]
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| - | [[Category: Rice]]
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| Structural highlights
Function
NLTP1_ORYSJ Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Nuclear magnetic resonance (NMR) spectroscopy was used to determine the three dimensional structure of rice nonspecific lipid transfer protein (ns-LTP), a 91 amino acid residue protein belonging to the broad family of plant ns-LTP. Sequence specific assignment was obtained for all but three HN backbone 1H resonances and for more than 95% of the 1H side-chain resonances using a combination of 1H 2D NOESY; TOCSY and COSY experiments at 293 K. The structure was calculated on the basis of four disulfide bridge restraints, 1259 distance constraints derived from 1H-1H Overhauser effects, 72 phi angle restraints and 32 hydrogen-bond restraints. The final solution structure involves four helices (H1: Cys3-Arg18, H2: Ala25-Ala37, H3: Thr41-Ala54 and H4: Ala66-Cys73) followed by a long C-terminal tail (T) with no observable regular structure. N-capping residues (Thr2, Ser24, Thr40), whose side-chain oxygen atoms are involved in hydrogen bonds with i + 3 amide proton additionally stabilize the N termini of the first three helices. The fourth helix involving Pro residues display a mixture of alpha and 3(10) conformation. The rms deviation of 14 final structures with respect to the average structure is 1.14 +/- 0.16 A for all heavy atoms (C, N, O and S) and 0.72 +/- 0.01 A for the backbone atoms. The global fold of rice ns-LTP is close to the previously published structures of wheat, barley and maize ns-LTPs exhibiting nearly identical pattern of the numerous sequence specific interactions. As reported previously for different four-helix topology proteins, hydrophobic, hydrogen bonding and electrostatic mechanisms of fold stabilization were found for the rice ns-LTP. The sequential alignment of 36 ns-LTP primary structures strongly suggests that there is a uniform pattern of specific long-range interactions (in terms of sequence), which stabilize the fold of all plant ns-LTPs.
Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins.,Poznanski J, Sodano P, Suh SW, Lee JY, Ptak M, Vovelle F Eur J Biochem. 1999 Feb;259(3):692-708. PMID:10092854[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Poznanski J, Sodano P, Suh SW, Lee JY, Ptak M, Vovelle F. Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins. Eur J Biochem. 1999 Feb;259(3):692-708. PMID:10092854
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