Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome.

The catalytic residue histidine 48 has been mutated to an alanine

Endoribonuclease involved in T4 mRNA inactivation

Solution Structure Analysis Of The Phage T4 Endoribonuclease Regb

RegB site-specific RNA endonuclease [Enterobacteria phage AR1]

unnamed protein product [Enterobacteria phage T4]

endoribonuclease [Enterobacteria phage T2]

endoribonuclease [Enterobacteria phage M1]

endoribonuclease [Enterobacteria phage K3]

endoribonuclease [Enterobacteria phage Ox2]

RegB site-specific RNA endonuclease [Enterobacteria phage T4]

site-specific RNase [Enterobacteria phage RB32]

site-specific RNase [Enterobacteria phage RB14]

site-specific RNase [Enterobacteria phage RB51]

site-specific RNA endonuclease [Enterobacteria phage T4T]

putative endoribonuclease [Shigella phage Shfl2]

site-specific RNA endonuclease [Enterobacteria phage vB_EcoM_ACG-C40]

RecName: Full=Endoribonuclease RegB; AltName: Full=Gp61.9

the three chemical shift files correspond to the three NOESY experiments used for structure determination. Two constraint files are non-assigned peak lists. One contains the assigned distance constraints and one the dihedral angle constraints
Chemical shift and constraint files for the RegB ribonuclease

ICSN-RMN, Antenne de l'ICSN a l'Ecole Polytechnique, CNRS

Institut Jacques Monod, CNRS et Universites Paris 6 et Paris 7

All Noesy were recorded with at least two mixing times (120 ms for assignement and 60 ms for structure determination)

mix of manual and automatic NOE assignment procedure
DIEP, CEA Saclay, 91191 Gif sur Yvette, France