1gq0: Difference between revisions
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==Solution structure of Antiamoebin I, a membrane channel-forming polypeptide; NMR, 20 structures== | ==Solution structure of Antiamoebin I, a membrane channel-forming polypeptide; NMR, 20 structures== | ||
<StructureSection load='1gq0' size='340' side='right' caption='[[1gq0 | <StructureSection load='1gq0' size='340' side='right'caption='[[1gq0]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gq0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1gq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Emericellopsis_sp._2723 Emericellopsis sp. 2723]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GQ0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </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>, <scene name='pdbligand=PRD_000161:Antiamoebin+1'>PRD_000161</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=1gq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gq0 OCA], [https://pdbe.org/1gq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gq0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gq0 ProSAT]</span></td></tr> | |||
<tr | </table> | ||
<table> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide.,Galbraith TP, Harris R, Driscoll PC, Wallace BA Biophys J. 2003 Jan;84(1):185-94. PMID:12524274<ref>PMID:12524274</ref> | Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide.,Galbraith TP, Harris R, Driscoll PC, Wallace BA Biophys J. 2003 Jan;84(1):185-94. PMID:12524274<ref>PMID:12524274</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1gq0" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Emericellopsis sp. 2723]] | [[Category: Emericellopsis sp. 2723]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Driscoll PC]] | ||
[[Category: | [[Category: Galbraith TP]] | ||
[[Category: | [[Category: Harris R]] | ||
[[Category: | [[Category: Wallace BA]] | ||
Latest revision as of 10:55, 3 May 2023
Solution structure of Antiamoebin I, a membrane channel-forming polypeptide; NMR, 20 structuresSolution structure of Antiamoebin I, a membrane channel-forming polypeptide; NMR, 20 structures
Structural highlights
Publication Abstract from PubMedAntiamoebin I is a membrane-active peptaibol produced by fungi of the species Emericellopsis which is capable of forming ion channels in membranes. Previous structure determinations by x-ray crystallography have shown the molecule is mostly helical, with a deep bend in the center of the polypeptide, and that the backbone structure is independent of the solvent used for crystallization. In this study, the solution structure of antiamoebin was determined by NMR spectroscopy in methanol, a solvent from which one of the crystal structures was determined. The ensemble of structures produced exhibit a right-handed helical C terminus and a left-handed helical conformation toward the N-terminus, in contrast to the completely right-handed helices found in the crystal structures. The NMR results also suggest that a "hinge" region exists, which gives flexibility to the polypeptide in the central region, and which could have functional implications for the membrane insertion process. A model for the membrane insertion and assembly process is proposed based on the antiamoebin solution and crystal structures, and is contrasted with the assembly and insertion mechanism proposed for other ion channel-forming polypeptides. Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide.,Galbraith TP, Harris R, Driscoll PC, Wallace BA Biophys J. 2003 Jan;84(1):185-94. PMID:12524274[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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