TY - JOUR
T1 - Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
AU - Korolev, Sergey
AU - Hsieh, John
AU - Gauss, George H.
AU - Lohman, Timothy M.
AU - Waksman, Gabriel
N1 - Funding Information:
We thank J. Kuriyan, G. Rose, I. Wong, J. Ali, P. Burgers, K. Hall, and S. Mathews for comments on the manuscript; T. Ho for synthesis and purification of the DNA; K. Bjornson, R. Gregorian, and I. Wong for contributing protein for crystallization; K. Fütterer for help in data collection; I. Wong for Figure 1 ; R. Pappu for Figure 8 ; and the staff of Beamline 7.1 at the Stanford Synchrotron Radiation Laboratory for assistance during synchrotron data collection. This work was supported by National Institutes of Health grants GM54033 to G. W. and GM45948 to T. M. L. Correspondence should be addressed to G. W. at waksman@gwiris1.wustl.edu.
PY - 1997/8/22
Y1 - 1997/8/22
N2 - Crystal structures of binary and ternary complexes of the E. coli Rep helicase bound to single-stranded (SS) DNA or ssDNA and ADP were determined to a resolution of 3.0 Å and 3.2 Å, respectively. The asymmetric unit in the crystals contains two Rep monomers differing from each other by a large reorientation of one of the domains, corresponding to a swiveling of 130°about a hinge region. Such domain movements are sufficiently large to suggest that these may be coupled to translocation of the Rep dimer along DNA. The ssDNA binding site involves the helicase motifs Ia, III, and V, whereas the ADP binding site involves helicase motifs I and IV. Residues in motifs II and VI may function to transduce the allosteric effects of nucleotides on DNA binding. These structures represent the first view of a 67 helicase bound to DNA.
AB - Crystal structures of binary and ternary complexes of the E. coli Rep helicase bound to single-stranded (SS) DNA or ssDNA and ADP were determined to a resolution of 3.0 Å and 3.2 Å, respectively. The asymmetric unit in the crystals contains two Rep monomers differing from each other by a large reorientation of one of the domains, corresponding to a swiveling of 130°about a hinge region. Such domain movements are sufficiently large to suggest that these may be coupled to translocation of the Rep dimer along DNA. The ssDNA binding site involves the helicase motifs Ia, III, and V, whereas the ADP binding site involves helicase motifs I and IV. Residues in motifs II and VI may function to transduce the allosteric effects of nucleotides on DNA binding. These structures represent the first view of a 67 helicase bound to DNA.
UR - http://www.scopus.com/inward/record.url?scp=0030740262&partnerID=8YFLogxK
U2 - 10.1016/S0092-8674(00)80525-5
DO - 10.1016/S0092-8674(00)80525-5
M3 - Article
C2 - 9288744
AN - SCOPUS:0030740262
SN - 0092-8674
VL - 90
SP - 635
EP - 647
JO - Cell
JF - Cell
IS - 4
ER -