5LWO

Structure of Spin-labelled T4 lysozyme mutant L115C-R119C-R1 at 100K

Summary for 5LWO

• Entry DOI: 10.2210/pdb5lwo/pdb
• Related: 5JDT
• Descriptor: Endolysin, [2,2,5,5-tetramethyl-3,4-bis(sulfanylmethyl)-2,5-dihydro-1H-pyrrol-1-yl]oxidanyl radical, CHLORIDE ION, ... (8 entities in total)
• Functional Keywords: nitroxide, spin label, t4 lysozyme, electron paramagnetic resonance, epr, hydrolase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 1
• Total formula weight: 19356.10

Authors

Loll, B.,Consentius, P.,Gohlke, U.,Mueller, R.,Kaupp, M.,Heinemann, U.,Wahl, M.C.,Risse, T. (deposition date: 2016-09-18, release date: 2017-03-08, Last modification date: 2024-04-03)

Primary citation

Consentius, P.,Loll, B.,Gohlke, U.,Alings, C.,Muller, C.,Muller, R.,Teutloff, C.,Heinemann, U.,Kaupp, M.,Wahl, M.C.,Risse, T.
Internal Dynamics of the 3-Pyrroline-N-Oxide Ring in Spin-Labeled Proteins.
J Phys Chem Lett, 8:1113-1117, 2017

PubMed Abstract: Site-directed spin labeling is a versatile tool to study structure as well as dynamics of proteins using EPR spectroscopy. Methanethiosulfonate (MTS) spin labels tethered through a disulfide linkage to an engineered cysteine residue were used in a large number of studies to extract structural as well as dynamic information on the protein from the rotational dynamics of the nitroxide moiety. The ring itself was always considered to be a rigid body. In this contribution, we present a combination of high-resolution X-ray crystallography and EPR spectroscopy of spin-labeled protein single crystals demonstrating that the nitroxide ring inverts fast at ambient temperature while exhibiting nonplanar conformations at low temperature. We have used quantum chemical calculations to explore the potential energy that determines the ring dynamics as well as the impact of the geometry on the magnetic parameters probed by EPR spectroscopy.

PubMed: 28221042
DOI: 10.1021/acs.jpclett.6b02971

Experimental method

X-RAY DIFFRACTION (1.183 Å)