1bb1
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(New page: 200px<br /><applet load="1bb1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bb1, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 21:50, 24 November 2007
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CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL
Overview
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.
About this Structure
1BB1 is a Protein complex structure of sequences from Synthetic construct with CL, ACE and NH2 as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a designed, thermostable, heterotrimeric coiled coil., Nautiyal S, Alber T, Protein Sci. 1999 Jan;8(1):84-90. PMID:10210186
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