View source for 2mal


==Solution structure of Lipid Transfer Protein from Lentil Lens Culinaris==
<StructureSection load='2mal' size='340' side='right'caption='[[2mal]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mal]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ljo 2ljo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mal OCA], [https://pdbe.org/2mal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mal RCSB], [https://www.ebi.ac.uk/pdbsum/2mal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mal ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NLTP2_LENCU NLTP2_LENCU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lipid transfer protein, designated as Lc-LTP2, was isolated from seeds of the lentil Lens culinaris. The protein has molecular mass 9282.7Da, consists of 93 amino acid residues including 8 cysteines forming 4 disulfide bonds. Lc-LTP2 and its stable isotope labeled analogues were overexpressed in Escherichia coli and purified. Antimicrobial activity of the recombinant protein was examined, and its spatial structure was studied by NMR spectroscopy. The polypeptide chain of Lc-LTP2 forms four alpha-helices (Cys4-Leu18, Pro26-Ala37, Thr42-Ala56, Thr64-Lys73) and a long C-terminal tail without regular secondary structure. Side chains of the hydrophobic residues form a relatively large internal tunnel-like lipid-binding cavity (van der Waals volume comes up to approximately 600A3). The side-chains of Arg45, Pro79, and Tyr80 are located near an assumed mouth of the cavity. Titration with dimyristoyl phosphatidylglycerol (DMPG) revealed formation of the Lc-LTP2/lipid non-covalent complex accompanied by rearrangements in the protein spatial structure and expansion of the internal cavity. The resultant Lc-LTP2/DMPG complex demonstrates limited lifetime and dissociates within tens of hours.

Recombinant production and solution structure of lipid transfer protein from lentil Lens culinaris.,Gizatullina AK, Finkina EI, Mineev KS, Melnikova DN, Bogdanov IV, Telezhinskaya IN, Balandin SV, Shenkarev ZO, Arseniev AS, Ovchinnikova TV Biochem Biophys Res Commun. 2013 Aug 31. pii: S0006-291X(13)01425-3. doi:, 10.1016/j.bbrc.2013.08.078. PMID:23998937<ref>PMID:23998937</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mal" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lens culinaris]]
[[Category: Gizatullina AK]]
[[Category: Mineev KS]]
[[Category: Shenkarev ZO]]