1coi
From Proteopedia
(New page: 200px<br /><applet load="1coi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1coi, resolution 2.1Å" /> '''DESIGNED TRIMERIC COI...) |
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| - | [[Image:1coi.jpg|left|200px]]<br /><applet load="1coi" size=" | + | [[Image:1coi.jpg|left|200px]]<br /><applet load="1coi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1coi, resolution 2.1Å" /> | caption="1coi, resolution 2.1Å" /> | ||
'''DESIGNED TRIMERIC COILED COIL-VALD'''<br /> | '''DESIGNED TRIMERIC COILED COIL-VALD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the 29-residue designed coiled coil | + | The three-dimensional structure of the 29-residue designed coiled coil having the amino acid sequence acetyl-E VEALEKK VAALESK VQALEKK VEALEHG-amide has been determined and refined to a crystallographic R-factor of 21.4% for all data from 10-A to 2.1-A resolution. This molecule is called coil-VaLd because it contains valine in the a heptad positions and leucine in the d heptad positions. In the trigonal crystal, three molecules, related by a crystallographic threefold axis, form a parallel three-helix bundle. The bundles are stacked head-to-tail to form a continuous coiled coil along the c-direction of the crystal. The contacts among the three helices within the coiled coil are mainly hydrophobic: four layers of valine residues alternate with four layers of leucine residues to form the core of the bundle. In contrast, mostly hydrophilic contacts mediate the interaction between trimers: here a total of two direct protein--protein hydrogen bonds are found. Based on the structure, we propose a scheme for designing crystals of peptides containing continuous two-, three-, and four-stranded coiled coils. |
==About this Structure== | ==About this Structure== | ||
| - | 1COI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] with SO4, ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1COI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
| - | [[Category: Degrado, W | + | [[Category: Degrado, W F.]] |
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
| - | [[Category: Ogihara, N | + | [[Category: Ogihara, N L.]] |
| - | [[Category: Weiss, M | + | [[Category: Weiss, M S.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
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[[Category: protein design]] | [[Category: protein design]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:07 2008'' |
Revision as of 10:08, 21 February 2008
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DESIGNED TRIMERIC COILED COIL-VALD
Overview
The three-dimensional structure of the 29-residue designed coiled coil having the amino acid sequence acetyl-E VEALEKK VAALESK VQALEKK VEALEHG-amide has been determined and refined to a crystallographic R-factor of 21.4% for all data from 10-A to 2.1-A resolution. This molecule is called coil-VaLd because it contains valine in the a heptad positions and leucine in the d heptad positions. In the trigonal crystal, three molecules, related by a crystallographic threefold axis, form a parallel three-helix bundle. The bundles are stacked head-to-tail to form a continuous coiled coil along the c-direction of the crystal. The contacts among the three helices within the coiled coil are mainly hydrophobic: four layers of valine residues alternate with four layers of leucine residues to form the core of the bundle. In contrast, mostly hydrophilic contacts mediate the interaction between trimers: here a total of two direct protein--protein hydrogen bonds are found. Based on the structure, we propose a scheme for designing crystals of peptides containing continuous two-, three-, and four-stranded coiled coils.
About this Structure
1COI is a Protein complex structure of sequences from Synthetic construct with , and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies., Ogihara NL, Weiss MS, Degrado WF, Eisenberg D, Protein Sci. 1997 Jan;6(1):80-8. PMID:9007979
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