1gq0: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
[[1gq0]] is a 1 chain structure with sequence from [http://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]. <br> | [[1gq0]] is a 1 chain structure with sequence from [http://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]. <br> | ||
<b>Related:</b> [[1joh|1joh]], [[1ee7|1ee7]], [[1amt|1amt]], [[1m24|1m24]], [[1ob4|1ob4]], [[1ob6|1ob6]], [[1ob7|1ob7]], [[1r9u|1r9u]], [[1ih9|1ih9]], [[1dlz|1dlz]]<br> | <b>[[Non-Standard_Residue|NonStd Res:]]</b> <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><br> | ||
<b>[[Related_structure|Related:]]</b> [[1joh|1joh]], [[1ee7|1ee7]], [[1amt|1amt]], [[1m24|1m24]], [[1ob4|1ob4]], [[1ob6|1ob6]], [[1ob7|1ob7]], [[1r9u|1r9u]], [[1ih9|1ih9]], [[1dlz|1dlz]]<br> | |||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gq0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gq0 RCSB], [http://www.ebi.ac.uk/pdbsum/1gq0 PDBsum]</span><br> | |||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Antiamoebin 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. | Antiamoebin 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. | ||