View source for 1dlz


==SOLUTION STRUCTURE OF THE CHANNEL-FORMER ZERVAMICIN IIB (PEPTAIBOL ANTIBIOTIC)==
<StructureSection load='1dlz' size='340' side='right'caption='[[1dlz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dlz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Emericellopsis_salmosynnemata Emericellopsis salmosynnemata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=DIV:D-ISOVALINE'>DIV</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</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=1dlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlz OCA], [https://pdbe.org/1dlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dlz RCSB], [https://www.ebi.ac.uk/pdbsum/1dlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dlz ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Spatial structure of the membrane channel-forming hexadecapeptide, zervamicin IIB, was studied by NMR spectroscopy in mixed solvents of different polarity ranging from CDCl3/CD3OH (9:1, v/v) to CD3OH/H2O (1:1, v/v). The results show that in all solvents used the peptide has a very similar structure that is a bent amphiphilic helix with a mean backbone root mean square deviation (rmsd) value of ca. 0.3 A. Side chains of Trp1, Ile2, Gln3, Ile5 and Thr6 are mobile. The results are discussed in relation to the validity of the obtained structure to serve as a building block of zervamicin IIB ion channels.

NMR structure of the channel-former zervamicin IIB in isotropic solvents.,Balashova TA, Shenkarev ZO, Tagaev AA, Ovchinnikova TV, Raap J, Arseniev AS FEBS Lett. 2000 Jan 28;466(2-3):333-6. PMID:10682854<ref>PMID:10682854</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dlz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Emericellopsis salmosynnemata]]
[[Category: Large Structures]]
[[Category: Arseniev AS]]
[[Category: Balashova TA]]
[[Category: Ovchinnikova TV]]
[[Category: Raap J]]
[[Category: Shenkarev ZO]]
[[Category: Tagaev AA]]