1bv2
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(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,...)
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Revision as of 09:49, 20 November 2007
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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
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