5JGX
Spin-Labeled T4 Lysozyme Construct V131V1
Summary for 5JGX
Entry DOI | 10.2210/pdb5jgx/pdb |
Related | 5JGN 5JGR 5JGU 5JGV 5JGZ |
Descriptor | Endolysin, CHLORIDE ION, POTASSIUM ION, ... (6 entities in total) |
Functional Keywords | spin label, epr, deer, hydrolase |
Biological source | Enterobacteria phage T4 sensu lato |
Total number of polymer chains | 1 |
Total formula weight | 19124.15 |
Authors | Balo, A.R.,Feyrer, H.,Ernst, O.P. (deposition date: 2016-04-20, release date: 2017-02-15, Last modification date: 2024-05-01) |
Primary citation | Balo, A.R.,Feyrer, H.,Ernst, O.P. Toward Precise Interpretation of DEER-Based Distance Distributions: Insights from Structural Characterization of V1 Spin-Labeled Side Chains. Biochemistry, 55:5256-5263, 2016 Cited by PubMed Abstract: Pulsed electron paramagnetic resonance experiments can measure individual distances between two spin-labeled side chains in proteins in the range of ∼1.5-8 nm. However, the flexibility of traditional spin-labeled side chains leads to diffuse spin density loci and thus distance distributions with relatively broad peaks, thereby complicating the interpretation of protein conformational states. Here we analyzed the spin-labeled V1 side chain, which is internally anchored and hence less flexible. Crystal structures of V1-labeled T4 lysozyme constructs carrying the V1 side chain on α-helical segments suggest that V1 side chains adopt only a few discrete rotamers. In most cases, only one rotamer is observed at a given site, explaining the frequently observed narrow distance distribution for doubly V1-labeled proteins. We used the present data to derive guidelines that may allow distance interpretation of other V1-labeled proteins for higher-precision structural modeling. PubMed: 27532325DOI: 10.1021/acs.biochem.6b00608 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.533 Å) |
Structure validation
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