1r9u
From Proteopedia
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|PDB= 1r9u |SIZE=350|CAPTION= <scene name='initialview01'>1r9u</scene> | |PDB= 1r9u |SIZE=350|CAPTION= <scene name='initialview01'>1r9u</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dlz|1DLZ]], [[1ih9|1IH9]], [[1gq0|1GQ0]], [[1joh|1JOH]], [[1amt|1AMT]], [[1ee7|1EE7]], [[1m24|1M24]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r9u OCA], [http://www.ebi.ac.uk/pdbsum/1r9u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r9u RCSB]</span> | ||
}} | }} | ||
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[[Category: Shenkarev, Z O.]] | [[Category: Shenkarev, Z O.]] | ||
[[Category: Yakimenko, Z A.]] | [[Category: Yakimenko, Z A.]] | ||
| - | [[Category: ACE]] | ||
[[Category: bent helix]] | [[Category: bent helix]] | ||
[[Category: bifurcated hydrogen bond]] | [[Category: bifurcated hydrogen bond]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:25:06 2008'' |
Revision as of 20:25, 30 March 2008
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| Ligands: | , , , , | ||||||
| Related: | 1DLZ, 1IH9, 1GQ0, 1JOH, 1AMT, 1EE7, 1M24
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Refined structure of peptaibol zervamicin IIB in methanol solution from trans-hydrogen bond J couplings
Overview
Zervamicin IIB (Zrv-IIB) is a channel-forming peptaibol antibiotic of fungal origin. The measured transhydrogen bond (3h)J(NC') couplings in methanol solution heaving average value of -0.41 Hz indicate that the stability of the Zrv-IIB helix in this milieu is comparable to the stability of helices in globular proteins. The N-terminus of the peptide forms an alpha-helix, whereas 3(10)-helical hydrogen bonds stabilize the C-terminus. However, two weak transhydrogen bond peaks are observed in a long-range HNCO spectrum for HN Aib(12). Energy calculations using the Empirical Conformation Energy Program for Peptides (ECEPP)/2 force field and the implicit solvent model show that the middle of the peptide helix accommodates a bifurcated hydrogen bond that is simultaneously formed between HN Aib(12) and CO Leu(8) and CO Aib(9). Several lowered (3h)J(NC') on a polar face of the helix correlate with the conformational exchange process observed earlier and imply dynamic distortions of a hydrogen bond pattern with the predominant population of a properly folded helical structure. The refined structure of Zrv-IIB on the basis of the observed hydrogen bond pattern has a small ( approximately 20 degrees ) angle of helix bending that is virtually identical to the angle of bending in dodecylphosphocholine (DPC) micelles, indicating the stability of a hinge region in different environments. NMR parameters ((1)HN chemical shifts and transpeptide bond (1)J(NC') couplings) sensitive to hydrogen bonding along with the solvent accessible surface area of carbonyl oxygens indicate a large polar patch on the convex side of the helix formed by three exposed backbone carbonyls of Aib(7), Aib(9), and Hyp(10) and polar side chains of Hyp(10), Gln(11), and Hyp(13). The unique structural features, high helix stability and the enhanced polar patch, set apart Zrv-IIB from other peptaibols (for example, alamethicin) and possibly underlie its biological and physiological properties.
About this Structure
1R9U is a Protein complex structure of sequences from Emericellopsis salmosynnemata. Full crystallographic information is available from OCA.
Reference
Peptaibol zervamicin IIb structure and dynamics refinement from transhydrogen bond J couplings., Shenkarev ZO, Balashova TA, Yakimenko ZA, Ovchinnikova TV, Arseniev AS, Biophys J. 2004 Jun;86(6):3687-99. PMID:15189865
Page seeded by OCA on Sun Mar 30 23:25:06 2008
