2RUJ

Solution structure of MTSL spin-labeled Schizosaccharomyces pombe Sin1 CRIM domain

Summary for 2RUJ

• Entry DOI: 10.2210/pdb2ruj/pdb
• Descriptor: Stress-activated map kinase-interacting protein 1 (1 entity in total)
• Functional Keywords: sin1, crim domain, torc2, pre, protein binding
• Biological source: Schizosaccharomyces pombe 972h- (Fission yeast)
• Total number of polymer chains: 1
• Total formula weight: 19243.36

Authors

Furuita, K.,Kataoka, S.,Sugiki, T.,Kobayashi, N.,Ikegami, T.,Shiozaki, K.,Fujiwara, T.,Kojima, C. (deposition date: 2014-07-24, release date: 2015-07-29, Last modification date: 2025-03-26)

Primary citation

Furuita, K.,Kataoka, S.,Sugiki, T.,Hattori, Y.,Kobayashi, N.,Ikegami, T.,Shiozaki, K.,Fujiwara, T.,Kojima, C.
Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints
J.Biomol.Nmr, 61:55-64, 2015

PubMed Abstract: NMR structure determination of soluble proteins depends in large part on distance restraints derived from NOE. In this study, we examined the impact of paramagnetic relaxation enhancement (PRE)-derived distance restraints on protein structure determination. A high-resolution structure of the loop-rich soluble protein Sin1 could not be determined by conventional NOE-based procedures due to an insufficient number of NOE restraints. By using the 867 PRE-derived distance restraints obtained from the NOE-based structure determination procedure, a high-resolution structure of Sin1 could be successfully determined. The convergence and accuracy of the determined structure were improved by increasing the number of PRE-derived distance restraints. This study demonstrates that PRE-derived distance restraints are useful in the determination of a high-resolution structure of a soluble protein when the number of NOE constraints is insufficient.

PubMed: 25428765
DOI: 10.1007/s10858-014-9882-7

Experimental method

SOLUTION NMR