1alz: Difference between revisions

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[[Image:1alz.gif|left|200px]]
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{{STRUCTURE_1alz|  PDB=1alz  |  SCENE=  }}
'''GRAMICIDIN D FROM BACILLUS BREVIS (ETHANOL SOLVATE)'''


==GRAMICIDIN D FROM BACILLUS BREVIS (ETHANOL SOLVATE)==
<StructureSection load='1alz' size='340' side='right'caption='[[1alz]], [[Resolution|resolution]] 0.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1alz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gma 1gma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALZ 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]] 0.86&#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=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=FVA:N-FORMYL-L-VALINE'>FVA</scene>, <scene name='pdbligand=PRD_000153:GRAMICIDIN+C'>PRD_000153</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=1alz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alz OCA], [https://pdbe.org/1alz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alz RCSB], [https://www.ebi.ac.uk/pdbsum/1alz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alz 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.


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gma 1gma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALZ OCA].
</div>
<div class="pdbe-citations 1alz" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Gramicidin|Gramicidin]]
[[Category: Burkhart, B M.]]
== References ==
[[Category: Duax, W L.]]
<references/>
[[Category: Langs, D A.]]
__TOC__
[[Category: Pangborn, W A.]]
</StructureSection>
[[Category: Peptide antibiotic]]
[[Category: Brevibacillus brevis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:26:06 2008''
[[Category: Large Structures]]
[[Category: Burkhart BM]]
[[Category: Duax WL]]
[[Category: Langs DA]]
[[Category: Pangborn WA]]

Latest revision as of 09:31, 19 July 2023

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

Structural highlights

1alz is a 2 chain structure with sequence from Brevibacillus brevis. This structure supersedes the now removed PDB entry 1gma. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 0.86Å
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

1alz, resolution 0.86Å

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