<HashMap><database>biostudies-other</database><scores/><additional><omics_type>Unknown</omics_type><volume>8(11)</volume><submitter>Kurinov IV</submitter><journal>Protein science : a publication of the Protein Society</journal><pagination>2399-405</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2144192</full_dataset_link><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.</abstract><repository>biostudies-other</repository><pmcid>PMC2144192</pmcid><data_source>Europe PMC</data_source><pubmed_authors>Venkatachalam TK</pubmed_authors><pubmed_authors>Rajamohan F</pubmed_authors><pubmed_authors>Uckun FM</pubmed_authors><pubmed_authors>Kurinov IV</pubmed_authors></additional><is_claimable>false</is_claimable><name>X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA.</name><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.</description><dates><release>1999-01-01T00:00:00Z</release><publication>1999 Nov</publication><modification>2019-03-27T02:22:13Z</modification><creation>2019-03-27T02:22:13Z</creation></dates><accession>S-EPMC2144192</accession><cross_references><pubmed>10595542</pubmed><doi>10.1110/ps.8.11.2399 </doi><pdb>1QCI</pdb><pdb>1QCG</pdb></cross_references></HashMap>