5KGR

Spin-Labeled T4 Lysozyme Construct I9V1/V131V1 (30 days)

Summary for 5KGR

• Entry DOI: 10.2210/pdb5kgr/pdb
• Related: 5JGN 5JGR 5JGU 5JGV 5JGX 5JGZ
• Descriptor: Endolysin, S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate, HEXANE-1,6-DIOL, ... (6 entities in total)
• Functional Keywords: spin label, epr, deer, hydrolase
• Biological source: Enterobacteria phage T4 sensu lato
• Cellular location: Host cytoplasm : P00720
• Total number of polymer chains: 1
• Total formula weight: 19388.68

Authors

Balo, A.R.,Feyrer, H.,Ernst, O.P. (deposition date: 2016-06-13, release date: 2017-02-15, Last modification date: 2024-10-30)

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

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: 27532325
DOI: 10.1021/acs.biochem.6b00608

Experimental method

X-RAY DIFFRACTION (1.473 Å)