1bv2

<StructureSection load='1bv2' size='340' side='right'caption='[[1bv2]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>

</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>

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== 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<ref>PMID:10092854</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1bv2" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lee, J Y]]

[[Category: Poznanski, J]]

[[Category: Ptak, M]]

[[Category: Sodano, P]]

[[Category: Suh, S W]]

[[Category: Vovelle, F]]

[[Category: Rice]]