File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site

TitleStructure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site
Authors
Issue Date2007
PublisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 2007, v. 35 n. 18, p. 6259-6267 How to Cite?
AbstractMaize ribosome-inactivating protein is classified as a class III or an atypical RNA N-glycosidase. It is synthesized as an inactive precursor with a 25-amino acid internal inactivation region, which is removed in the active form. As the first structural example of this class of proteins, crystals of the precursor and the active form were diffracted to 2.4 and 2.5 Å, respectively. The two proteins are similar, with main chain root mean square deviation (RMSD) of 0.519. In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long α-helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake. Like bacterial ribosome-inactivating proteins, maize ribosome-inactivating protein does not have a back-up glutamate in the active site, which helps the protein to retain some activity if the catalytic glutamate is mutated. The structure reveals that the active site is too small to accommodate two glutamate residues. Our structure suggests that maize ribosome-inactivating protein may represent an intermediate product in the evolution of ribosome-inactivating proteins. © 2007 The Author(s).
Persistent Identifierhttp://hdl.handle.net/10722/157493
ISSN
2015 Impact Factor: 9.202
2015 SCImago Journal Rankings: 7.458
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMak, ANSen_US
dc.contributor.authorWong, YTen_US
dc.contributor.authorAn, YJen_US
dc.contributor.authorCha, SSen_US
dc.contributor.authorSze, KHen_US
dc.contributor.authorAu, SWNen_US
dc.contributor.authorWong, KBen_US
dc.contributor.authorShaw, PCen_US
dc.date.accessioned2012-08-08T08:50:31Z-
dc.date.available2012-08-08T08:50:31Z-
dc.date.issued2007en_US
dc.identifier.citationNucleic Acids Research, 2007, v. 35 n. 18, p. 6259-6267en_US
dc.identifier.issn0305-1048en_US
dc.identifier.urihttp://hdl.handle.net/10722/157493-
dc.description.abstractMaize ribosome-inactivating protein is classified as a class III or an atypical RNA N-glycosidase. It is synthesized as an inactive precursor with a 25-amino acid internal inactivation region, which is removed in the active form. As the first structural example of this class of proteins, crystals of the precursor and the active form were diffracted to 2.4 and 2.5 Å, respectively. The two proteins are similar, with main chain root mean square deviation (RMSD) of 0.519. In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long α-helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake. Like bacterial ribosome-inactivating proteins, maize ribosome-inactivating protein does not have a back-up glutamate in the active site, which helps the protein to retain some activity if the catalytic glutamate is mutated. The structure reveals that the active site is too small to accommodate two glutamate residues. Our structure suggests that maize ribosome-inactivating protein may represent an intermediate product in the evolution of ribosome-inactivating proteins. © 2007 The Author(s).en_US
dc.languageengen_US
dc.publisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/en_US
dc.relation.ispartofNucleic Acids Researchen_US
dc.rightsNucleic Acids Research. Copyright © Oxford University Press.-
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCell Line, Tumoren_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshGlutamic Acid - Chemistry - Geneticsen_US
dc.subject.meshHumansen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMutationen_US
dc.subject.meshPlant Proteins - Chemistry - Genetics - Pharmacologyen_US
dc.subject.meshProtein Synthesis Inhibitors - Chemistry - Metabolism - Pharmacologyen_US
dc.subject.meshRatsen_US
dc.subject.meshRibosomal Proteins - Metabolismen_US
dc.subject.meshRibosome Inactivating Proteins - Chemistry - Genetics - Pharmacologyen_US
dc.subject.meshRibosomes - Chemistryen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.titleStructure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active siteen_US
dc.typeArticleen_US
dc.identifier.emailSze, KH: khsze@hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1093/nar/gkm687en_US
dc.identifier.pmid17855394-
dc.identifier.pmcidPMC2094058-
dc.identifier.scopuseid_2-s2.0-35548984395en_US
dc.identifier.hkuros142714-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-35548984395&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume35en_US
dc.identifier.issue18en_US
dc.identifier.spage6259en_US
dc.identifier.epage6267en_US
dc.identifier.isiWOS:000250683600034-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridMak, ANS=36780323900en_US
dc.identifier.scopusauthoridWong, YT=22942688400en_US
dc.identifier.scopusauthoridAn, YJ=7102051166en_US
dc.identifier.scopusauthoridCha, SS=7201864593en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.scopusauthoridAu, SWN=7005457819en_US
dc.identifier.scopusauthoridWong, KB=7404759301en_US
dc.identifier.scopusauthoridShaw, PC=35599523600en_US
dc.customcontrol.immutablesml 130528-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats