1al4: Difference between revisions
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== Structural highlights == | == 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> | <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='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 | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.13Å</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> | <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> | </table> | ||
Latest revision as of 02:47, 21 November 2024
GRAMICIDIN D FROM BACILLUS BREVIS (N-PROPANOL SOLVATE)GRAMICIDIN D FROM BACILLUS BREVIS (N-PROPANOL SOLVATE)
Structural highlights
Publication Abstract from PubMedThe 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 AlsoReferences |
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