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New page: left|200px<br /><applet load="1al4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1al4, resolution 1.13Å" /> '''GRAMICIDIN D FROM BA...
 
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[[Image:1al4.jpg|left|200px]]<br /><applet load="1al4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1al4, resolution 1.13&Aring;" />
'''GRAMICIDIN D FROM BACILLUS BREVIS (N-PROPANOL SOLVATE)'''<br />


==Overview==
==GRAMICIDIN D FROM BACILLUS BREVIS (N-PROPANOL SOLVATE)==
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.
<StructureSection load='1al4' size='340' side='right'caption='[[1al4]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1al4]] 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=1AL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AL4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.13&#8491;</td></tr>
<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=POL:N-PROPANOL'>POL</scene>, <scene name='pdbligand=QIL:N-FORMYL-L-ISOLEUCINE'>QIL</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=1al4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al4 OCA], [https://pdbe.org/1al4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1al4 RCSB], [https://www.ebi.ac.uk/pdbsum/1al4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1al4 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.


==About this Structure==
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>
1AL4 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 POL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AL4 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9788907 9788907]
</div>
<div class="pdbe-citations 1al4" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Gramicidin|Gramicidin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brevibacillus brevis]]
[[Category: Brevibacillus brevis]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Burkhart, B.M.]]
[[Category: Burkhart BM]]
[[Category: Duax, W.L.]]
[[Category: Duax WL]]
[[Category: Gassman, R.M.]]
[[Category: Gassman RM]]
[[Category: Pangborn, W.A.]]
[[Category: Pangborn WA]]
[[Category: POL]]
[[Category: peptide antibiotic]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:00:50 2007''

Latest revision as of 23:47, 20 November 2024

GRAMICIDIN D FROM BACILLUS BREVIS (N-PROPANOL SOLVATE)

1al4, resolution 1.13Å

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