Publication:
Structural analysis of the elongation factor G protein from the low-temperature-adapted bacterium Arthrobacter globiformis S155

dc.contributor.author Berchet, Veronica en_US
dc.contributor.author Thomas, Torsten en_US
dc.contributor.author Cavicchioli, Ricardo en_US
dc.contributor.author Russell, Nicholas en_US
dc.contributor.author Gounot, Anne-Marie en_US
dc.date.accessioned 2021-11-25T13:25:00Z
dc.date.available 2021-11-25T13:25:00Z
dc.date.issued 2000 en_US
dc.description.abstract The first structural analysis of elongation factor G (EF-G) from a cold-adapted bacterium is presented. EF-G is an essential protein involved in the elongation process during protein synthesis and is therefore thought to play a crucial role in the low-temperature adaptation of cold-adapted microorganisms. To define its importance, the EF-G gene (fus) from the psychrotolerant bacterium Arthrobacter globiformis SI55 was cloned and sequenced. The deduced primary structure of the elongation factor is composed of 700 amino acids with a predicted molecular mass of 77.4 kDa. A three-dimensional model of the protein was constructed based on the known crystal structures of structurally homologous proteins. Structural features that might potentially be important for activity and flexibility at low temperature were deduced by comparisons with models of the EF-G proteins from the closely related mesophiles Micrococcus luteus and Mycobacterium tuberculosis. These features include a loss in the number of salt bridges in intradomain and interdomain positions, increased solvent interactions mediated by greater charge and polarity on domain surfaces, loop insertions, loss of proline residues in loop structures, and an increase of hydrophobicity in core regions. Specific changes have also been identified in the catalytic domain (G domain) and sites of potential ribosome interaction, which may directly affect guanosine triphosphate (GTP) hydrolysis and elongation rates at low temperature. en_US
dc.identifier.issn 1431-0651 en_US
dc.identifier.uri http://hdl.handle.net/1959.4/39583
dc.language English
dc.language.iso EN en_US
dc.rights CC BY-NC-ND 3.0 en_US
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/3.0/au/ en_US
dc.source Legacy MARC en_US
dc.title Structural analysis of the elongation factor G protein from the low-temperature-adapted bacterium Arthrobacter globiformis S155 en_US
dc.type Journal Article en
dcterms.accessRights metadata only access
dspace.entity.type Publication en_US
unsw.accessRights.uri http://purl.org/coar/access_right/c_14cb
unsw.identifier.doiPublisher http://dx.doi.org/10.1007/s007920050146 en_US
unsw.relation.faculty Science
unsw.relation.ispartofissue 2 en_US
unsw.relation.ispartofjournal Extremophiles en_US
unsw.relation.ispartofpagefrompageto 123-130 en_US
unsw.relation.ispartofvolume 4 en_US
unsw.relation.originalPublicationAffiliation Berchet, Veronica en_US
unsw.relation.originalPublicationAffiliation Thomas, Torsten, Biotechnology & Biomolecular Sciences, Faculty of Science, UNSW en_US
unsw.relation.originalPublicationAffiliation Cavicchioli, Ricardo, Biotechnology & Biomolecular Sciences, Faculty of Science, UNSW en_US
unsw.relation.originalPublicationAffiliation Russell, Nicholas en_US
unsw.relation.originalPublicationAffiliation Gounot, Anne-Marie en_US
unsw.relation.school School of Biotechnology & Biomolecular Sciences *
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