1ih9
From Proteopedia
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| - | [[Image:1ih9.jpg|left|200px]] | + | [[Image:1ih9.jpg|left|200px]] |
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| - | '''NMR Structure of Zervamicin IIB (peptaibol antibiotic) Bound to DPC Micelles''' | + | {{Structure |
| + | |PDB= 1ih9 |SIZE=350|CAPTION= <scene name='initialview01'>1ih9</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR Structure of Zervamicin IIB (peptaibol antibiotic) Bound to DPC Micelles''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IH9 is a [ | + | 1IH9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Emericellopsis_salmosynnemata Emericellopsis salmosynnemata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IH9 OCA]. |
==Reference== | ==Reference== | ||
| - | Spatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gating., Shenkarev ZO, Balashova TA, Efremov RG, Yakimenko ZA, Ovchinnikova TV, Raap J, Arseniev AS, Biophys J. 2002 Feb;82(2):762-71. PMID:[http:// | + | Spatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gating., Shenkarev ZO, Balashova TA, Efremov RG, Yakimenko ZA, Ovchinnikova TV, Raap J, Arseniev AS, Biophys J. 2002 Feb;82(2):762-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11806918 11806918] |
[[Category: Emericellopsis salmosynnemata]] | [[Category: Emericellopsis salmosynnemata]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: bent helix]] | [[Category: bent helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:20 2008'' |
Revision as of 09:50, 20 March 2008
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NMR Structure of Zervamicin IIB (peptaibol antibiotic) Bound to DPC Micelles
Overview
Zervamicin IIB is a 16-amino acid peptaibol that forms voltage-dependent ion channels with multilevel conductance states in planar lipid bilayers and vesicular systems. The spatial structure of zervamicin IIB bound to dodecylphosphocholine micelles was studied by nuclear magnetic resonance spectroscopy. The set of 20 structures obtained has a bent helical conformation with a mean backbone root mean square deviation value of approximately 0.2 A and resembles the structure in isotropic solvents (Balashova et al., 2000. NMR structure of the channel-former zervamicin IIB in isotropic solvents. FEBS Lett 466:333-336). The N-terminus represents an alpha-helix, whereas the C-terminal part has a mixed 3(10)/alpha(R) hydrogen-bond pattern. In the anisotropic micelle environment, the bending angle on Hyp10 (23 degrees) is smaller than that (47 degrees) in isotropic solvents. In the NOESY (Nuclear Overhauser Effect Spectroscopy) spectra, the characteristic attenuation of the peptide signals by 5- and 16-doxylstearate relaxation probes indicates a peripheral mode of the peptaibol binding to the micelle with the N-terminus immersed slightly deeper into micelle interior. Analysis of the surface hydrophobicity reveals that the zervamicin IIB helix is amphiphilic and well suited to formation of a tetrameric transmembrane bundle, according to the barrel-stave mechanism. The results are discussed in a context of voltage-driven peptaibol insertion into membrane.
About this Structure
1IH9 is a Protein complex structure of sequences from Emericellopsis salmosynnemata. Full crystallographic information is available from OCA.
Reference
Spatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gating., Shenkarev ZO, Balashova TA, Efremov RG, Yakimenko ZA, Ovchinnikova TV, Raap J, Arseniev AS, Biophys J. 2002 Feb;82(2):762-71. PMID:11806918
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