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3wkr
From Proteopedia
(Difference between revisions)
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| - | ==Crystal structure of | + | ==Crystal structure of the SepCysS-SepCysE complex from Methanocaldococcus jannaschii== |
<StructureSection load='3wkr' size='340' side='right' caption='[[3wkr]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3wkr' size='340' side='right' caption='[[3wkr]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wkr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wkr RCSB], [http://www.ebi.ac.uk/pdbsum/3wkr PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wkr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wkr RCSB], [http://www.ebi.ac.uk/pdbsum/3wkr PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Methanogenic archaea lack cysteinyl-tRNA synthetase; they synthesize Cys-tRNA and cysteine in a tRNA-dependent manner. Two enzymes are required: Phosphoseryl-tRNA synthetase (SepRS) forms phosphoseryl-tRNA(Cys) (Sep-tRNA(Cys)), which is converted to Cys-tRNA(Cys) by Sep-tRNA:Cys-tRNA synthase (SepCysS). This represents the ancestral pathway of Cys biosynthesis and coding in archaea. Here we report a translation factor, SepCysE, essential for methanococcal Cys biosynthesis; its deletion in Methanococcus maripaludis causes Cys auxotrophy. SepCysE acts as a scaffold for SepRS and SepCysS to form a stable high-affinity complex for tRNA(Cys) causing a 14-fold increase in the initial rate of Cys-tRNA(Cys) formation. Based on our crystal structure (2.8-A resolution) of a SepCysSSepCysE complex, a SepRSSepCysESepCysS structure model suggests that this ternary complex enables substrate channeling of Sep-tRNA(Cys). A phylogenetic analysis suggests coevolution of SepCysE with SepRS and SepCysS in the last universal common ancestral state. Our findings suggest that the tRNA-dependent Cys biosynthesis proceeds in a multienzyme complex without release of the intermediate and this mechanism may have facilitated the addition of Cys to the genetic code. | ||
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| + | Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.,Liu Y, Nakamura A, Nakazawa Y, Asano N, Ford KA, Hohn MJ, Tanaka I, Yao M, Soll D Proc Natl Acad Sci U S A. 2014 Jul 22;111(29):10520-5. doi:, 10.1073/pnas.1411267111. Epub 2014 Jul 7. PMID:25002468<ref>PMID:25002468</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:33, 30 July 2014
Crystal structure of the SepCysS-SepCysE complex from Methanocaldococcus jannaschii
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