1alx: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
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'''GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL SOLVATE)'''<br />


==Overview==
==GRAMICIDIN D FROM BACILLUS BREVIS (METHANOL 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='1alx' size='340' side='right'caption='[[1alx]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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.


==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>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ALX 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 1alx" 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: 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://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:02:47 2007''

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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