From Proteopedia
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| - | [[Image:1bv2.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1bv2| PDB=1bv2 | SCENE= }} | | {{STRUCTURE_1bv2| PDB=1bv2 | SCENE= }} |
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| - | '''LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES'''
| + | ===LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10092854}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10092854 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10092854}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1BV2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BV2 OCA]. | + | 1BV2 is a [[Single protein]] structure of 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]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Nmr]] | | [[Category: Nmr]] |
| | [[Category: Rice]] | | [[Category: Rice]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:59:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:45:51 2008'' |
Revision as of 16:45, 30 June 2008
Template:STRUCTURE 1bv2
LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES
Template:ABSTRACT PUBMED 10092854
About this Structure
1BV2 is a Single protein structure of sequence from Oryza sativa. Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Mon Jun 30 19:45:51 2008
