1W5H

An anti-parallel four helix bundle.

Summary for 1W5H

• Entry DOI: 10.2210/pdb1w5h/pdb
• Related: 1CE9 1DGC 1ENV 1FAV 1GCL 1GCM 1GK6 1GZL 1IHQ 1IJ0 1IJ1 1IJ2 1IJ3 1KQL 1LD4 1LLM 1M6T 1NKN 1PIQ 1RB1 1RB4 1RB5 1RB6 1SWI 1TMZ 1UNT 1UNU 1UNV 1UNW 1UNX 1UNY 1UNZ 1UO0 1UO1 1UO2 1UO3 1UO4 1UO5 1VZL 1W5G 1W5I 1W5J 1W5K 1W5L 1YSA 1ZII 1ZIJ 1ZIK 1ZIL 1ZIM 1ZTA 2DGC 2ZTA
• Descriptor: GENERAL CONTROL PROTEIN GCN4 (1 entity in total)
• Functional Keywords: four helix bundle, antiparallel four helix bundle
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 2
• Total formula weight: 7991.60

Authors

Yadav, M.K.,Leman, L.J.,Stout, C.D.,Ghadiri, M.R. (deposition date: 2004-08-06, release date: 2004-09-24, Last modification date: 2024-05-08)

Primary citation

Yadav, M.K.,Leman, L.J.,Price, D.J.,Brooks, C.L.,Stout, C.D.,Ghadiri, M.R.
Coiled Coils at the Edge of Configurational Heterogeneity. Structural Analyses of Parallel and Antiparallel Homotetrameric Coiled Coils Reveal Configurational Sensitivity to a Single Solvent-Exposed Amino Acid Substitution.
Biochemistry, 45:4463-, 2006

PubMed Abstract: A detailed understanding of the mechanisms by which particular amino acid sequences can give rise to more than one folded structure, such as for proteins that undergo large conformational changes or misfolding, is a long-standing objective of protein chemistry. Here, we describe the crystal structures of a single coiled-coil peptide in distinct parallel and antiparallel tetrameric configurations and further describe the parallel or antiparallel crystal structures of several related peptide sequences; the antiparallel tetrameric assemblies represent the first crystal structures of GCN4-derived peptides exhibiting such a configuration. Intriguingly, substitution of a single solvent-exposed residue enabled the parallel coiled-coil tetramer GCN4-pLI to populate the antiparallel configuration, suggesting that the two configurations are close enough in energy for subtle sequence changes to have important structural consequences. We present a structural analysis of the small changes to the helix register and side-chain conformations that accommodate the two configurations and have supplemented these results using solution studies and a molecular dynamics energetic analysis using a replica exchange methodology. Considering the previous examples of structural nonspecificity in coiled-coil peptides, the findings reported here not only emphasize the predisposition of the coiled-coil motif to adopt multiple configurations but also call attention to the associated risk that observed crytstal structures may not represent the only (or even the major) species present in solution.

PubMed: 16584182
DOI: 10.1021/BI060092Q

Experimental method

X-RAY DIFFRACTION (2.5 Å)