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[[Image:1alx.gif|left|200px]]


{{Structure
==GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)==
|PDB= 1alx |SIZE=350|CAPTION= <scene name='initialview01'>1alx</scene>, resolution 1.20&Aring;
<StructureSection load='1alx' size='340' side='right'caption='[[1alx]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene> and <scene name='pdbligand=MOH:METHANOL'>MOH</scene>
<table><tr><td colspan='2'>[[1alx]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALX FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=FVA:N-FORMYL-L-VALINE'>FVA</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=PRD_000152:GRAMICIDIN+D'>PRD_000152</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1alx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alx OCA], [https://pdbe.org/1alx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alx RCSB], [https://www.ebi.ac.uk/pdbsum/1alx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)'''
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<ref>PMID:9788907</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1alx" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Gramicidin|Gramicidin]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==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://www.ncbi.nlm.nih.gov/pubmed/9788907 9788907]
[[Category: Brevibacillus brevis]]
[[Category: Brevibacillus brevis]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Burkhart, B M.]]
[[Category: Burkhart BM]]
[[Category: Courseille, C.]]
[[Category: Courseille C]]
[[Category: Duax, W L.]]
[[Category: Duax WL]]
[[Category: Hospital, M.]]
[[Category: Hospital M]]
[[Category: Langs, D A.]]
[[Category: Langs DA]]
[[Category: Pangborn, W A.]]
[[Category: Pangborn WA]]
[[Category: Precigoux, G.]]
[[Category: Precigoux G]]
[[Category: Smith, G D.]]
[[Category: Smith GD]]
[[Category: FOR]]
[[Category: MOH]]
[[Category: peptide antibiotic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:19 2008''

Latest revision as of 13:53, 2 August 2023

GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)

Structural highlights

1alx is a 2 chain structure with sequence from Brevibacillus brevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Burkhart BM, Gassman RM, Langs DA, Pangborn WA, Duax WL. Heterodimer formation and crystal nucleation of gramicidin D. Biophys J. 1998 Nov;75(5):2135-46. PMID:9788907

1alx, resolution 1.20Å

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