1m24: Difference between revisions
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<StructureSection load='1m24' size='340' side='right' caption='[[1m24]], [[Resolution|resolution]] 0.90Å' scene=''> | <StructureSection load='1m24' size='340' side='right' caption='[[1m24]], [[Resolution|resolution]] 0.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m24]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1m24]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_viride Trichoderma viride]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M24 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M24 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=VOL:L-VALINOL'>VOL</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=VOL:L-VALINOL'>VOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r9u|1r9u]], [[1dlz|1dlz]], [[1ih9|1ih9]], [[1gq0|1gq0]], [[1joh|1joh]], [[1amt|1amt]], [[1ee7|1ee7]], [[1ob7|1ob7]], [[1ob6|1ob6]], [[1ob4|1ob4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r9u|1r9u]], [[1dlz|1dlz]], [[1ih9|1ih9]], [[1gq0|1gq0]], [[1joh|1joh]], [[1amt|1amt]], [[1ee7|1ee7]], [[1ob7|1ob7]], [[1ob6|1ob6]], [[1ob4|1ob4]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m24 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m24 RCSB], [http://www.ebi.ac.uk/pdbsum/1m24 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m24 OCA], [http://pdbe.org/1m24 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m24 RCSB], [http://www.ebi.ac.uk/pdbsum/1m24 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1m24" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Trichoderma viride]] | ||
[[Category: Brueckner, H]] | [[Category: Brueckner, H]] | ||
[[Category: Chugh, J K]] | [[Category: Chugh, J K]] | ||
Revision as of 01:40, 10 September 2015
Trichotoxin_A50E, An Ion Channel-Forming PolypeptideTrichotoxin_A50E, An Ion Channel-Forming Polypeptide
Structural highlights
Publication Abstract from PubMedTrichotoxin_A50E is an 18-residue peptaibol antibiotic which forms multimeric transmembrane channels through self-association. The crystal structure of trichotoxin has been determined at a resolution of 0.9 A. The trichotoxin sequence contains nine helix-promoting Aib residues, which contribute to the formation of an entirely helical structure that has a central bend of 8-10 degrees located between residues 10-13. Trichotoxin is the first solved structure of the peptaibol family that is all alpha-helix as opposed to containing part or all 3(10)-helix. Gln residues in positions 6 and 17 produce a polar face, and are proposed to form the channel lumen. An octameric model channel has been constructed from the crystal structure. It has a central pore of approximately 4-5 A radius, a size sufficient to enable transport of ions, with a constricted region at one end, formed by a ring of Gln6 residues. Electrostatic calculations are consistent with it being a cationic channel. Model for a helical bundle channel based on the high-resolution crystal structure of trichotoxin_A50E.,Chugh JK, Bruckner H, Wallace BA Biochemistry. 2002 Oct 29;41(43):12934-41. PMID:12390019[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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