1alz: Difference between revisions

Revision as of 12:46, 21 February 2008

GRAMICIDIN D FROM BACILLUS BREVIS (ETHANOL SOLVATE)

OverviewOverview

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 StructureAbout this Structure

1ALZ is a Protein complex structure of sequences from Brevibacillus brevis with as ligand. This structure supersedes the now removed PDB entry 1GMA. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 11:46:01 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1alz.gif|left|200px]]<br /><applet load="1alz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1alz.gif|left|200px]]<br /><applet load="1alz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1alz, resolution 0.86&Aring;" />
 '''GRAMICIDIN D FROM BACILLUS BREVIS (ETHANOL SOLVATE)'''<br />
 ==Overview==
-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.
+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==
-ALZ 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 EOH as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1GMA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ALZ OCA].
+ALZ 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 <scene name='pdbligand=EOH:'>EOH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1GMA. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALZ OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Brevibacillus brevis]]
 [[Category: Protein complex]]
-[[Category: Burkhart, B.M.]]
+[[Category: Burkhart, B M.]]
-[[Category: Duax, W.L.]]
+[[Category: Duax, W L.]]
-[[Category: Langs, D.A.]]
+[[Category: Langs, D A.]]
-[[Category: Pangborn, W.A.]]
+[[Category: Pangborn, W A.]]
 [[Category: EOH]]
 [[Category: peptide antibiotic]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:03:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:01 2008''