2odr: Difference between revisions
New page: left|200px<br /><applet load="2odr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2odr, resolution 3.228Å" /> '''Methanococcus Marip... |
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==Overview== | ==Overview== | ||
A number of archaeal organisms generate Cys-tRNA(Cys) in a two-step | 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-A 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 II, alpha(4) synthetase whose quaternary structure arrangement of subunits closely resembles that of the heterotetrameric (alphabeta)(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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Kamtekar, S.]] | [[Category: Kamtekar, S.]] | ||
[[Category: Steitz, T | [[Category: Steitz, T A.]] | ||
[[Category: phosphoserine trna synthetase class ii]] | [[Category: phosphoserine trna synthetase class ii]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:27 2008'' | ||
Revision as of 19:17, 21 February 2008
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Methanococcus Maripaludis Phosphoseryl-tRNA synthetase
OverviewOverview
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-A 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 II, alpha(4) synthetase whose quaternary structure arrangement of subunits closely resembles that of the heterotetrameric (alphabeta)(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.
About this StructureAbout this Structure
2ODR is a Protein complex structure of sequences from Methanococcus maripaludis. Full crystallographic information is available from OCA.
ReferenceReference
Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase., Kamtekar S, Hohn MJ, Park HS, Schnitzbauer M, Sauerwald A, Soll D, Steitz TA, Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2620-5. Epub 2007 Feb 14. PMID:17301225
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