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Title: Structural Studies of HHARI/UbcH7~Ub Reveal Unique E2~Ub Conformational Restriction by RBR RING1

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NIHHHMI
OSTI Identifier:
1390859
Resource Type:
Journal Article
Resource Relation:
Journal Name: Structure; Journal Volume: 25; Journal Issue: 6
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Dove, Katja K., Olszewski, Jennifer L., Martino, Luigi, Duda, David M., Wu, Xiaoli S., Miller, Darcie J., Reiter, Katherine H., Rittinger, Katrin, Schulman, Brenda A., and Klevit, Rachel E.. Structural Studies of HHARI/UbcH7~Ub Reveal Unique E2~Ub Conformational Restriction by RBR RING1. United States: N. p., 2017. Web. doi:10.1016/j.str.2017.04.013.
Dove, Katja K., Olszewski, Jennifer L., Martino, Luigi, Duda, David M., Wu, Xiaoli S., Miller, Darcie J., Reiter, Katherine H., Rittinger, Katrin, Schulman, Brenda A., & Klevit, Rachel E.. Structural Studies of HHARI/UbcH7~Ub Reveal Unique E2~Ub Conformational Restriction by RBR RING1. United States. doi:10.1016/j.str.2017.04.013.
Dove, Katja K., Olszewski, Jennifer L., Martino, Luigi, Duda, David M., Wu, Xiaoli S., Miller, Darcie J., Reiter, Katherine H., Rittinger, Katrin, Schulman, Brenda A., and Klevit, Rachel E.. 2017. "Structural Studies of HHARI/UbcH7~Ub Reveal Unique E2~Ub Conformational Restriction by RBR RING1". United States. doi:10.1016/j.str.2017.04.013.
@article{osti_1390859,
title = {Structural Studies of HHARI/UbcH7~Ub Reveal Unique E2~Ub Conformational Restriction by RBR RING1},
author = {Dove, Katja K. and Olszewski, Jennifer L. and Martino, Luigi and Duda, David M. and Wu, Xiaoli S. and Miller, Darcie J. and Reiter, Katherine H. and Rittinger, Katrin and Schulman, Brenda A. and Klevit, Rachel E.},
abstractNote = {},
doi = {10.1016/j.str.2017.04.013},
journal = {Structure},
number = 6,
volume = 25,
place = {United States},
year = 2017,
month = 6
}
  • No abstract prepared.
  • Escherichia coli DNA topoisomerase III belongs to the type IA family of DNA topoisomerases, which transiently cleave single-stranded DNA (ssDNA) via a 5{prime} phosphotyrosine intermediate. We have solved crystal structures of wild-type E. coli topoisomerase III bound to an eight-base ssDNA molecule in three different pH environments. The structures reveal the enzyme in three distinct conformational states while bound to DNA. One conformation resembles the one observed previously with a DNA-bound, catalytically inactive mutant of topoisomerase III where DNA binding realigns catalytic residues to form a functional active site. Another conformation represents a novel intermediate in which DNA is boundmore » along the ssDNA-binding groove but does not enter the active site, which remains in a catalytically inactive, closed state. A third conformation shows an intermediate state where the enzyme is still in a closed state, but the ssDNA is starting to invade the active site. For the first time, the active site region in the presence of both the catalytic tyrosine and ssDNA substrate is revealed for a type IA DNA topoisomerase, although there is no evidence of ssDNA cleavage. Comparative analysis of the various conformational states suggests a sequence of domain movements undertaken by the enzyme upon substrate binding.« less
  • The H NMR spectra of a series of blood group A active oligosaccharides containing from four to ten sugar residues have been completely assigned, and quantitative nuclear Overhauser enhancements (NOE) have been measured between protons separated by known distances within the pyranoside ring. The observation of NOE between anomeric protons and those of the aglycon sugar as well as small effects between protons of distant rings suggests that the oligosaccharides have well-defined conformations. Conformational energy calculations were carried out on a trisaccharide, Fuc( -1 2)(GalNAc( -1 3))-GalUS -O-me, which models the nonreducing terminal fragments of the blood group A oligosaccharides.more » The results of calculations with three different potential energy functions which have been widely used in peptides and carbohydrates gave several minimum energy conformations. In NOE calculations from conformational models, the rotational correlation time was adjusted to fit T1's and intra-ring NOE. Comparison of calculated maps of NOE as a function of glycosidic dihedral angles showed that only a small region of conformational space was consistent with experimental data on a blood group A tetrasaccharide alditol. This conformation occurs at an energy minimum in all three energy calculations. Temperature dependence of the NOE implies that the oligosaccharides adopt single rigid conformations which do not change with temperature.« less