2rbi: Difference between revisions

Members of the microbial guanyl-specific ribonuclease family catalyse the, endonucleolytic cleavage of single-stranded RNA in a two-step reaction, involving transesterification to form a 2',3'-cyclic phosphate and its, subsequent hydrolysis to yield the respective 3'-phosphate. The, extracellular ribonuclease from Bacillus intermedius (binase, RNase Bi), shares a common mechanism for RNA hydrolysis with mammalian RNases. Two, catalytic residues in the active site of binase, Glu72 and His101, are, thought to be involved in general acid-general base catalysis of RNA, cleavage. Using site-directed mutagenesis, binase mutants were produced, containing amino acid substitutions H101N and H101T and their catalytic, properties towards RNA, poly(I), poly(A), GpC and guanosine 2',3'-cyclic, phosphate (cGMP) substrates were studied. The engineered mutant proteins, are active in the transesterification step which produces the 2',3'-cyclic, phosphate species but they have lost the ability to catalyse hydrolysis of, the cyclic phosphate to give the 3' monophosphate product.

2RBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Structure known Active Sites: 1, 2 and 3. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2RBI OCA].  

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 12:31:45 2007''