EC Number   |
Reference |
|---|
    2.7.6.5 | cryo-EM structure of RelA in complex with the Escherichia coli 70S ribosome with an average resolution of 3.7 A. RelA adopts an open conformation, where the C-terminal domain is intertwined around an A/T-like tRNA within the intersubunit cavity of the ribosome and the N-terminal domain extends into the solvent |
762036 |
| 2.7.6.5 | nucleotide-free Rel has an elongated conformation in which the TGS domain contacts the synthesis domain by an interface involving alpha-helix 14 and beta strands 7/8 of the synthesis and TGS domains, respectively |
760841 |
| 2.7.6.5 | purified enzyme in presence of ATP and GTP, 1 week, X-ray diffraction structure determination and analysis at 2.94 A resolution |
739546 |
| 2.7.6.5 | structures of RelP in pre-catalytic state (bound to GTP and adenosine 5'-(alpha,beta-methylene)triphosphate), and post-catalytic state (bound to pppGpp). RelP forms a tetramer, but unlike RelQ (SAS1), it is strongly inhibited by both pppGpp and ppGpp and is insensitive to inhibition by RNA. The active site pocket is formed mainly by the beta-strands and the loops beta1/alpha2,alpha3/beta2, and beta3/beta4 in addition to two small helices, alpha2 and alpha5. pppGpp adopts different conformations inside the two active sites (chains A and B) of the dimer |
761487 |
| 2.7.6.5 | the crystallographic asymmetric unit contains two copies of RelSeq 1-385, two catalytic domains are clearly evident within each monomer, with the hydrolase (residues 5-159) and the synthetase (residues 176-371) domains joined by an overlapping central 3-helix bundle (residues 135-195) |
661439 |
