1COI

DESIGNED TRIMERIC COILED COIL-VALD

Summary for 1COI

• Entry DOI: 10.2210/pdb1coi/pdb
• Descriptor: COIL-VALD, SULFATE ION (3 entities in total)
• Functional Keywords: alpha-helical bundle, protein design, coiled coil design
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 3302.77

Authors

Ogihara, N.L.,Weiss, M.S.,Degrado, W.F.,Eisenberg, D. (deposition date: 1996-08-10, release date: 1997-02-12, Last modification date: 2024-10-23)

Primary citation

Ogihara, N.L.,Weiss, M.S.,Degrado, W.F.,Eisenberg, D.
The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies.
Protein Sci., 6:80-88, 1997

PubMed Abstract: 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.

PubMed: 9007979

Experimental method

X-RAY DIFFRACTION (2.1 Å)