Structure of the [beta] subunit of translation initiation factor 2 from the Archaeon Methanococcus jannaschii by NMR : a representative of the eIF2[beta]/eIF5 family of proteins

Simple item page
dc.contributor.advisorHoffman, David W., Ph. D.en
dc.contributor.advisorSalazar, Miguelen
dc.creatorCho, Seongeunen
dc.date.accessioned2011-04-18T21:02:53Zen
dc.date.available2011-04-18T21:02:53Zen
dc.date.issued2002-05en
dc.descriptiontexten
dc.description.abstracteIF2b is one of the three subunits of eukaryotic initiation factor 2 (eIF2), a protein which recruits the initiator Met-tRNA and GTP to the 40S ribosomal subunit as part of the 43S pre-initiation complex. The three dimensional structure of aIF2b from Methanococcus jannaschii, an archaeal homologue of eIF2, was determined using multidimensional NMR methods. The aIF2b was found to consist of two independent structural domains. The N-terminal domain contains a four-stranded antiparallel b sheet and two a helices on one side of the sheet. The folding topology was found to be similar to that of the DNA-binding domain of a yeast heat shock transcription factor and a domain within the ribosomal protein S4, although there is no significant homology at the level of primary sequence. The C-terminal domain of aIF2b contains a 'zinc ribbon' motif of three antiparallel b strands, with four conserved cysteines arranged as two CXXC units separated by 17 residues. The role of zinc in the C-terminal domain was investigated with a synthetic peptide that corresponds to the last 50 amino acid residues (residues 94-143) of aIF2b. The N- and Cterminal domains of aIF2b are connected by a helical linker, and were found to be independent of each other. Conserved residues on the surface of each domain that are likely candidates for direct interaction with other components of the translational apparatus were identified. The significant primary sequence homology between archaeal aIF2b and the eukaryotic initiation factors eIF2b and eIF5 allows structural features to be predicted for these latter two proteins from this first structural model of aIF2b.
dc.description.departmentPharmaceutical Sciencesen
dc.format.mediumelectronicen
dc.identifier.urihttp://hdl.handle.net/2152/10939en
dc.language.isoengen
dc.rightsCopyright is held by the author. Presentation of this material on the Libraries' web site by University Libraries, The University of Texas at Austin was made possible under a limited license grant from the author who has retained all copyrights in the works.en
dc.rights.restrictionRestricteden
dc.subjectProteins--Analysisen
dc.subjectNuclear magnetic responseen
dc.titleStructure of the [beta] subunit of translation initiation factor 2 from the Archaeon Methanococcus jannaschii by NMR : a representative of the eIF2[beta]/eIF5 family of proteinsen
thesis.degree.departmentPharmacyen
thesis.degree.disciplinePharmacyen
thesis.degree.grantorThe University of Texas at Austinen
thesis.degree.levelDoctoralen
thesis.degree.nameDoctor of Philosophyen

Access full-text files

Original bundle

Now showing 1 - 1 of 1
No Thumbnail Available
Name:
chos022.pdf
Size:
2.3 MB
Format:
Adobe Portable Document Format
Description:
Restricted to EID users
Download

License bundle

Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.66 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

UT Electronic Theses and Dissertations