1alx
From Proteopedia
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| - | [[Image:1alx.gif|left|200px]] | + | [[Image:1alx.gif|left|200px]] |
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| - | '''GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)''' | + | {{Structure |
| + | |PDB= 1alx |SIZE=350|CAPTION= <scene name='initialview01'>1alx</scene>, resolution 1.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene> and <scene name='pdbligand=MOH:METHANOL'>MOH</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ALX is a [ | + | 1ALX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALX OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9788907 9788907] |
[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
| - | ''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 09:59:19 2008'' |
Revision as of 07:59, 20 March 2008
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| , resolution 1.20Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 09:59:19 2008
