2odr: Difference between revisions

Revision as of 06:47, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2odr.png

Template:STRUCTURE 2odr

Methanococcus Maripaludis Phosphoseryl-tRNA synthetaseMethanococcus Maripaludis Phosphoseryl-tRNA synthetase

Template:ABSTRACT PUBMED 17301225

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

Page seeded by OCA on Mon Jul 28 06:46:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2odr.jpg|left|200px]]
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-'''Methanococcus Maripaludis Phosphoseryl-tRNA synthetase'''
+===Methanococcus Maripaludis Phosphoseryl-tRNA synthetase===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17301225}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17301225 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17301225}}
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 [[Category: Steitz, T A.]]
 [[Category: Phosphoserine trna synthetase class ii]]
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