1bv2
From Proteopedia
(New page: 200px<br /><applet load="1bv2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bv2" /> '''LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR,...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bv2.gif|left|200px]]<br /><applet load="1bv2" size=" | + | [[Image:1bv2.gif|left|200px]]<br /><applet load="1bv2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bv2" /> | caption="1bv2" /> | ||
'''LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES'''<br /> | '''LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nuclear magnetic resonance (NMR) spectroscopy was used to determine the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1BV2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http:// | + | 1BV2 is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Oryza sativa]] | [[Category: Oryza sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lee, J | + | [[Category: Lee, J Y.]] |
[[Category: Poznanski, J.]] | [[Category: Poznanski, J.]] | ||
[[Category: Ptak, M.]] | [[Category: Ptak, M.]] | ||
[[Category: Sodano, P.]] | [[Category: Sodano, P.]] | ||
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: Vovelle, F.]] | [[Category: Vovelle, F.]] | ||
[[Category: lipid transfer protein]] | [[Category: lipid transfer protein]] | ||
| Line 25: | Line 25: | ||
[[Category: rice]] | [[Category: rice]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:27 2008'' |
Revision as of 09:59, 21 February 2008
|
LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES
Overview
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.
About this Structure
1BV2 is a Single protein structure of sequence from Oryza sativa. Full crystallographic 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 Thu Feb 21 11:59:27 2008
