2XJ3

High resolution structure of the T55C mutant of CylR2.

Summary for 2XJ3

• Entry DOI: 10.2210/pdb2xj3/pdb
• Related: 1UTX 2XI8 2XIU
• Descriptor: CYLR2 SYNONYM CYTOLYSIN REPRESSOR 2, GLYCEROL (3 entities in total)
• Functional Keywords: dna binding protein, hth-dna binding motif, transcription regulator
• Biological source: ENTEROCOCCUS FAECALIS
• Total number of polymer chains: 2
• Total formula weight: 15638.24

Authors

Gruene, T.,Cho, M.K.,Karyagina, I.,Kim, H.Y.,Grosse, C.,Giller, K.,Zweckstetter, M.,Becker, S. (deposition date: 2010-07-02, release date: 2011-02-09, Last modification date: 2023-12-20)

Primary citation

Gruene, T.,Cho, M.K.,Karyagina, I.,Kim, H.Y.,Grosse, C.,Giller, K.,Zweckstetter, M.,Becker, S.
Integrated Analysis of the Conformation of a Protein-Linked Spin Label by Crystallography, Epr and NMR Spectroscopy.
J.Biomol.NMR, 49:111-, 2011

PubMed Abstract: Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of globular, modular and intrinsically disordered proteins, as well as protein-protein and protein-DNA complexes. Here we characterized the conformation of a spin-label attached to the homodimeric protein CylR2 using a combination of X-ray crystallography, electron paramagnetic resonance (EPR) and NMR spectroscopy. Close agreement was found between the conformation of the spin label observed in the crystal structure with interspin distances measured by EPR and signal broadening in NMR spectra, suggesting that the conformation seen in the crystal structure is also preferred in solution. In contrast, conformations of the spin label observed in crystal structures of T4 lysozyme are not in agreement with the paramagnetic relaxation enhancement observed for spin-labeled CylR2 in solution. Our data demonstrate that accurate positioning of the paramagnetic center is essential for high-resolution structure determination.

PubMed: 21271275
DOI: 10.1007/S10858-011-9471-Y

Experimental method

X-RAY DIFFRACTION (1.23 Å)