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1coi
From Proteopedia
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|PDB= 1coi |SIZE=350|CAPTION= <scene name='initialview01'>1coi</scene>, resolution 2.1Å | |PDB= 1coi |SIZE=350|CAPTION= <scene name='initialview01'>1coi</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1coi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1coi OCA], [http://www.ebi.ac.uk/pdbsum/1coi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1coi RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Ogihara, N L.]] | [[Category: Ogihara, N L.]] | ||
[[Category: Weiss, M S.]] | [[Category: Weiss, M S.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NH2]] | ||
| - | [[Category: SO4]] | ||
[[Category: alpha-helical bundle]] | [[Category: alpha-helical bundle]] | ||
[[Category: coiled coil design]] | [[Category: coiled coil design]] | ||
[[Category: protein design]] | [[Category: protein design]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:31 2008'' |
Revision as of 16:25, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 19:25:31 2008
