4TL1

GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 10

Summary for 4TL1

• Entry DOI: 10.2210/pdb4tl1/pdb
• Descriptor: General control protein GCN4, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: coiled coil, transcription
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 8111.62

Authors

Tavenor, N.A.,Silva, K.I.,Saxena, S.,Horne, W.S. (deposition date: 2014-05-28, release date: 2014-08-06, Last modification date: 2023-09-27)

Primary citation

Tavenor, N.A.,Silva, K.I.,Saxena, S.,Horne, W.S.
Origins of Structural Flexibility in Protein-Based Supramolecular Polymers Revealed by DEER Spectroscopy.
J.Phys.Chem.B, 118:9881-9889, 2014

PubMed Abstract: Modular assembly of bio-inspired supramolecular polymers is a powerful technique to develop new soft nanomaterials, and protein folding is a versatile basis for preparing such materials. Previous work demonstrated a significant difference in the physical properties of closely related supramolecular polymers composed of building blocks in which identical coiled-coil-forming peptides are cross-linked by one of two subtly different organic linkers (one flexible and the other rigid). Herein, we investigate the molecular basis for this observation by isolating a single subunit of the supramolecular polymer chain and probing its structure and conformational flexibility by double electron-electron resonance (DEER) spectroscopy. Experimental spin-spin distance distributions for two different labeling sites coupled with molecular dynamics simulations provide insights into how the linker structure impacts chain dynamics in the coiled-coil supramolecular polymer.

PubMed: 25060334
DOI: 10.1021/jp505643w

Experimental method

X-RAY DIFFRACTION (1.8 Å)