{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(11)"],"submitter":["Kurinov IV"],"journal":["Protein science : a publication of the Protein Society"],"pagination":["2399-405"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2144192"],"abstract":["Pokeweed antiviral protein (PAP) is a ribosome-inactivating protein (RIP), which enzymatically removes a single adenine base from a conserved, surface exposed loop sequence of ribosomal rRNA. We now present unprecedented experimental evidence that PAP can release not only adenine but guanine as well from Escherichia coli rRNA, albeit at a rate 20 times slower than for adenine. We also report X-ray structure analysis and supporting modeling studies for the interactions of PAP with guanine. Our modeling studies indicated that PAP can accommodate a guanine base in the active site pocket without large conformational changes. This prediction was experimentally confirmed, since a guanine base was visible in the active site pocket of the crystal structure of the PAP-guanine complex."],"repository":["biostudies-other"],"pmcid":["PMC2144192"],"data_source":["Europe PMC"],"pubmed_authors":["Venkatachalam TK","Rajamohan F","Uckun FM","Kurinov IV"],"additional_accession":[]},"is_claimable":false,"name":"X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA.","description":"Pokeweed antiviral protein (PAP) is a ribosome-inactivating protein (RIP), which enzymatically removes a single adenine base from a conserved, surface exposed loop sequence of ribosomal rRNA. We now present unprecedented experimental evidence that PAP can release not only adenine but guanine as well from Escherichia coli rRNA, albeit at a rate 20 times slower than for adenine. We also report X-ray structure analysis and supporting modeling studies for the interactions of PAP with guanine. Our modeling studies indicated that PAP can accommodate a guanine base in the active site pocket without large conformational changes. This prediction was experimentally confirmed, since a guanine base was visible in the active site pocket of the crystal structure of the PAP-guanine complex.","dates":{"release":"1999-01-01T00:00:00Z","publication":"1999 Nov","modification":"2019-03-27T02:22:13Z","creation":"2019-03-27T02:22:13Z"},"accession":"S-EPMC2144192","cross_references":{"pubmed":["10595542"],"doi":["10.1110/ps.8.11.2399 "],"pdb":["1QCI","1QCG"]}}