DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kamtekar, S | ko |
dc.contributor.author | Hohn, MJ | ko |
dc.contributor.author | Park, Hee-Sung | ko |
dc.contributor.author | Schnitzbauer, M | ko |
dc.contributor.author | Sauerwald, A | ko |
dc.contributor.author | Soll, D | ko |
dc.contributor.author | Steitz, TA | ko |
dc.date.accessioned | 2013-03-07T16:12:11Z | - |
dc.date.available | 2013-03-07T16:12:11Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2007-02 | - |
dc.identifier.citation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.104, no.8, pp.2620 - 2625 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | http://hdl.handle.net/10203/90653 | - |
dc.description.abstract | A number of archaeal organisms generate Cys-tRNA(Cys) in a two-step pathway, first charging phosphoserine (Sep) onto tRNA(Cys) and subsequently converting it to Cys-tRNA(Cys). We have determined, at 3.2-angstrom resolution, the structure of the Methanococcus maripaludis phosphoseryl-tRNA synthetase (SepRS), which catalyzes the first step of this pathway. The structure shows that SepRS is a class 11, alpha 4 synthetase whose quaternary structure arrangement of subunits closely resembles that of the heterotetrameric (alpha beta)(2) phenylalanyl-tRNA synthetase (PheRS). Homology modeling of a tRNA complex indicates that, in contrast to PheRS, a single monomer in the SepRS tetramer may recognize both the acceptor terminus and anticodon of a tRNA substrate. Using a complex with tungstate as a marker for the position of the phosphate moiety of Sep, we suggest that SepRS and PheRS bind their respective amino acid substrates in dissimilar orientations by using different residues. | - |
dc.language | English | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.subject | AMINOACYL-TRANSFER-RNA | - |
dc.subject | PHENYLALANYL-ADENYLATE | - |
dc.subject | THERMUS-THERMOPHILUS | - |
dc.subject | GENETIC-CODE | - |
dc.subject | BINDING FOLD | - |
dc.subject | EVOLUTION | - |
dc.subject | REVEALS | - |
dc.subject | DOMAIN | - |
dc.subject | COMPLEX | - |
dc.subject | ACID | - |
dc.title | Toward understanding phosphoseryl-tRNA(Cys) formation: The crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase | - |
dc.type | Article | - |
dc.identifier.wosid | 000244511200013 | - |
dc.identifier.scopusid | 2-s2.0-33847257897 | - |
dc.type.rims | ART | - |
dc.citation.volume | 104 | - |
dc.citation.issue | 8 | - |
dc.citation.beginningpage | 2620 | - |
dc.citation.endingpage | 2625 | - |
dc.citation.publicationname | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.identifier.doi | 10.1073/pnas.0611504104 | - |
dc.contributor.localauthor | Park, Hee-Sung | - |
dc.contributor.nonIdAuthor | Kamtekar, S | - |
dc.contributor.nonIdAuthor | Hohn, MJ | - |
dc.contributor.nonIdAuthor | Schnitzbauer, M | - |
dc.contributor.nonIdAuthor | Sauerwald, A | - |
dc.contributor.nonIdAuthor | Soll, D | - |
dc.contributor.nonIdAuthor | Steitz, TA | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | cysteine | - |
dc.subject.keywordAuthor | methanogen | - |
dc.subject.keywordAuthor | phosphoserine | - |
dc.subject.keywordAuthor | archaea | - |
dc.subject.keywordAuthor | aminoacyl-tRNA synthetase | - |
dc.subject.keywordPlus | AMINOACYL-TRANSFER-RNA | - |
dc.subject.keywordPlus | PHENYLALANYL-ADENYLATE | - |
dc.subject.keywordPlus | THERMUS-THERMOPHILUS | - |
dc.subject.keywordPlus | GENETIC-CODE | - |
dc.subject.keywordPlus | BINDING FOLD | - |
dc.subject.keywordPlus | EVOLUTION | - |
dc.subject.keywordPlus | REVEALS | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | ACID | - |
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