1BB1

CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL

Summary for 1BB1

• Entry DOI: 10.2210/pdb1bb1/pdb
• Descriptor: DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: de novo protein design, coiled coil
• Biological source: synthetic construct; More
• Total number of polymer chains: 3
• Total formula weight: 11246.58

Authors

Nautiyal, S.,Alber, T. (deposition date: 1998-04-28, release date: 1999-02-02, Last modification date: 2024-10-16)

Primary citation

Nautiyal, S.,Alber, T.
Crystal structure of a designed, thermostable, heterotrimeric coiled coil.
Protein Sci., 8:84-90, 1999

PubMed Abstract: Electrostatic interactions are often critical for determining the specificity of protein-protein complexes. To study the role of electrostatic interactions for assembly of helical bundles, we previously designed a thermostable, heterotrimeric coiled coil, ABC, in which charged residues were employed to drive preferential association of three distinct, 34-residue helices. To investigate the basis for heterotrimer specificity, we have used multiwavelength anomalous diffraction (MAD) analysis to determine the 1.8 A resolution crystal structure of ABC. The structure shows that ABC forms a heterotrimeric coiled coil with the intended arrangement of parallel chains. Over half of the ion pairs engineered to restrict helix associations were apparent in the experimental electron density map. As seen in other trimeric coiled coils, ABC displays acute knobs-into-holes packing and a buried anion coordinated by core polar amino acids. These interactions validate the design strategy and illustrate how packing and polar contacts determine structural uniqueness.

PubMed: 10210186

Experimental method

X-RAY DIFFRACTION (1.8 Å)