2ruj

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

spinqualitylabelsall models 2ruj Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ruj is a 1 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 10 models Ligands: R1A Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SIN1_SCHPO Interacts with the sty1 MAP kinase and has a role in the timing of the initiation of mitosis. Publication Abstract from PubMed 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. Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints.,Furuita K, Kataoka S, Sugiki T, Hattori Y, Kobayashi N, Ikegami T, Shiozaki K, Fujiwara T, Kojima C J Biomol NMR. 2015 Jan;61(1):55-64. doi: 10.1007/s10858-014-9882-7. Epub 2014 Nov, 27. PMID:25428765 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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