3wks

Crystal structure of the SepCysS-SepCysE N-terminal domain complex fromCrystal structure of the SepCysS-SepCysE N-terminal domain complex from

Structural highlights

3wks is a 4 chain structure with sequence from Metja. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	3wkr
Gene:	MJ1678 (METJA), MJ1481 (METJA)
Activity:	O-phospho-L-seryl-tRNA:Cys-tRNA synthase, with EC number 2.5.1.73
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPSS_METJA] Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).^[1]

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sauerwald A, Zhu W, Major TA, Roy H, Palioura S, Jahn D, Whitman WB, Yates JR 3rd, Ibba M, Soll D. RNA-dependent cysteine biosynthesis in archaea. Science. 2005 Mar 25;307(5717):1969-72. PMID:15790858 doi:http://dx.doi.org/10.1126/science.1108329
↑ Liu Y, Nakamura A, Nakazawa Y, Asano N, Ford KA, Hohn MJ, Tanaka I, Yao M, Soll D. Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea. 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 doi:http://dx.doi.org/10.1073/pnas.1411267111

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OCA

[1] Sauerwald A, Zhu W, Major TA, Roy H, Palioura S, Jahn D, Whitman WB, Yates JR 3rd, Ibba M, Soll D. RNA-dependent cysteine biosynthesis in archaea. Science. 2005 Mar 25;307(5717):1969-72. PMID:15790858 doi:http://dx.doi.org/10.1126/science.1108329

[2] Liu Y, Nakamura A, Nakazawa Y, Asano N, Ford KA, Hohn MJ, Tanaka I, Yao M, Soll D. Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea. 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 doi:http://dx.doi.org/10.1073/pnas.1411267111

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