2fcn: Difference between revisions
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[[Image:2fcn.gif|left|200px]] | [[Image:2fcn.gif|left|200px]] | ||
'''X-ray Crystal Structure of a Chemically Synthesized [D-Val35]Ubiquitin with a Cubic Space Group''' | {{Structure | ||
|PDB= 2fcn |SIZE=350|CAPTION= <scene name='initialview01'>2fcn</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''X-ray Crystal Structure of a Chemically Synthesized [D-Val35]Ubiquitin with a Cubic Space Group''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2FCN is a [ | 2FCN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCN OCA]. | ||
==Reference== | ==Reference== | ||
Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis., Bang D, Gribenko AV, Tereshko V, Kossiakoff AA, Kent SB, Makhatadze GI, Nat Chem Biol. 2006 Mar;2(3):139-43. Epub 2006 Jan 30. PMID:[http:// | Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis., Bang D, Gribenko AV, Tereshko V, Kossiakoff AA, Kent SB, Makhatadze GI, Nat Chem Biol. 2006 Mar;2(3):139-43. Epub 2006 Jan 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16446709 16446709] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bang, D.]] | [[Category: Bang, D.]] | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:50:47 2008'' | ||
Revision as of 17:50, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray Crystal Structure of a Chemically Synthesized [D-Val35]Ubiquitin with a Cubic Space Group
OverviewOverview
The alpha-helix is a fundamental protein structural motif and is frequently terminated by a glycine residue. Explanations for the predominance of glycine at the C-cap terminal portions of alpha-helices have invoked uniquely favorable energetics of this residue in a left-handed conformation or enhanced solvation of the peptide backbone because of the absence of a side chain. Attempts to quantify the contributions of these two effects have been made previously, but the issue remains unresolved. Here we have used chemical protein synthesis to dissect the energetic basis of alpha-helix termination by comparing a series of ubiquitin variants containing an L-amino acid or the corresponding D-amino acid at the C-cap Gly35 position. D-Amino acids can adopt a left-handed conformation without energetic penalty, so the contributions of conformational strain and backbone solvation can thus be separated. Analysis of the thermodynamic data revealed that the preference for glycine at the C' position of a helix is predominantly a conformational effect.
About this StructureAbout this Structure
2FCN is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis., Bang D, Gribenko AV, Tereshko V, Kossiakoff AA, Kent SB, Makhatadze GI, Nat Chem Biol. 2006 Mar;2(3):139-43. Epub 2006 Jan 30. PMID:16446709
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