1alx
From Proteopedia
(New page: 200px<br /><applet load="1alx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1alx, resolution 1.20Å" /> '''GRAMICIDIN D FROM BA...) |
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| - | [[Image:1alx.gif|left|200px]]<br /><applet load="1alx" size=" | + | [[Image:1alx.gif|left|200px]]<br /><applet load="1alx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1alx, resolution 1.20Å" /> | caption="1alx, resolution 1.20Å" /> | ||
'''GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)'''<br /> | '''GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The linear pentadecapeptide antibiotic gramicidin D is a heterogeneous | + | The linear pentadecapeptide antibiotic gramicidin D is a heterogeneous mixture of six components. Precise refinements of three-dimensional structures of naturally occurring gramicidin D in crystals obtained from methanol, ethanol, and n-propanol demonstrate the unexpected presence of stable left-handed antiparallel double-helical heterodimers that vary with the crystallization solvent. The side chains of Trp residues in the three structures exhibit sequence-specific patterns of conformational preference. Tyr substitution for Trp at position 11 appears to favor beta ribbon formation and stabilization of the antiparallel double helix that acts as a template for gramicidin folding and nucleation of different crystal forms. The fact that a minor component in a heterogeneous mixture influences aggregation and crystal nucleation has potential applications to other systems in which anomalous behavior is exhibited by aggregation of apparently homogeneous materials, such as the enigmatic behavior of prion proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1ALX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis] with FOR and MOH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ALX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis] with <scene name='pdbligand=FOR:'>FOR</scene> and <scene name='pdbligand=MOH:'>MOH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Burkhart, B | + | [[Category: Burkhart, B M.]] |
[[Category: Courseille, C.]] | [[Category: Courseille, C.]] | ||
| - | [[Category: Duax, W | + | [[Category: Duax, W L.]] |
[[Category: Hospital, M.]] | [[Category: Hospital, M.]] | ||
| - | [[Category: Langs, D | + | [[Category: Langs, D A.]] |
| - | [[Category: Pangborn, W | + | [[Category: Pangborn, W A.]] |
[[Category: Precigoux, G.]] | [[Category: Precigoux, G.]] | ||
| - | [[Category: Smith, G | + | [[Category: Smith, G D.]] |
[[Category: FOR]] | [[Category: FOR]] | ||
[[Category: MOH]] | [[Category: MOH]] | ||
[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:53 2008'' |
Revision as of 09:45, 21 February 2008
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GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)
Overview
The linear pentadecapeptide antibiotic gramicidin D is a heterogeneous mixture of six components. Precise refinements of three-dimensional structures of naturally occurring gramicidin D in crystals obtained from methanol, ethanol, and n-propanol demonstrate the unexpected presence of stable left-handed antiparallel double-helical heterodimers that vary with the crystallization solvent. The side chains of Trp residues in the three structures exhibit sequence-specific patterns of conformational preference. Tyr substitution for Trp at position 11 appears to favor beta ribbon formation and stabilization of the antiparallel double helix that acts as a template for gramicidin folding and nucleation of different crystal forms. The fact that a minor component in a heterogeneous mixture influences aggregation and crystal nucleation has potential applications to other systems in which anomalous behavior is exhibited by aggregation of apparently homogeneous materials, such as the enigmatic behavior of prion proteins.
About this Structure
1ALX is a Protein complex structure of sequences from Brevibacillus brevis with and as ligands. Full crystallographic information is available from OCA.
Reference
Heterodimer formation and crystal nucleation of gramicidin D., Burkhart BM, Gassman RM, Langs DA, Pangborn WA, Duax WL, Biophys J. 1998 Nov;75(5):2135-46. PMID:9788907
Page seeded by OCA on Thu Feb 21 11:45:53 2008
