View source for 3sbn


==trichovirin I-4A in polar environment at 0.9 Angstroem==
<StructureSection load='3sbn' size='340' side='right'caption='[[3sbn]], [[Resolution|resolution]] 0.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sbn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_viride Trichoderma viride]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.9&#8491;</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=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=DCL:2-AMINO-4-METHYL-PENTAN-1-OL'>DCL</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=PRD_000828:Trichovirin+I-4A'>PRD_000828</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=3sbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbn OCA], [https://pdbe.org/3sbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbn RCSB], [https://www.ebi.ac.uk/pdbsum/3sbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbn ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The first crystal structure of a member of peptaibol antibiotic subfamily 4, trichovirin I-4A (14 residues), has been determined by direct methods and refined at atomic resolution. The monoclinic unit cell has two molecules in the asymmetric unit. Both molecules assume a 3(10) right-handed helical conformation and are significantly bent. The molecules pack loosely along the crystallographic twofold axis, forming two large tunnels between symmetry-related molecules in which no ordered solvent could be located. Carbonyl O atoms which are not involved in intramolecular hydrogen bonding participate in close van der Waals interactions with apolar groups. The necessary amphipathicity for biological activity of peptaibols is not realised in the crystal structure. Hence, a structural change of trichovirin to an alpha-helical conformation is proposed for membrane integration and efficient water/ion transportation across the lipid bilayer.

Four complete turns of a curved 3(10)-helix at atomic resolution: the crystal structure of the peptaibol trichovirin I-4A in a polar environment suggests a transition to alpha-helix for membrane function.,Gessmann R, Axford D, Owen RL, Bruckner H, Petratos K Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):109-16. Epub 2012, Jan 6. PMID:22281739<ref>PMID:22281739</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3sbn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Trichoderma viride]]
[[Category: Axford D]]
[[Category: Gessmann R]]
[[Category: Petratos K]]