1coi
From Proteopedia
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| - | [[Image:1coi.jpg|left|200px]] | + | [[Image:1coi.jpg|left|200px]] |
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| - | '''DESIGNED TRIMERIC COILED COIL-VALD''' | + | {{Structure |
| + | |PDB= 1coi |SIZE=350|CAPTION= <scene name='initialview01'>1coi</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DESIGNED TRIMERIC COILED COIL-VALD''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1COI is a [ | + | 1COI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9007979 9007979] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
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[[Category: protein design]] | [[Category: protein design]] | ||
| - | ''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 10:26:59 2008'' |
Revision as of 08:27, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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