3wks

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'''Unreleased structure'''
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==Crystal structure of the SepCysS-SepCysE N-terminal domain complex from==
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<StructureSection load='3wks' size='340' side='right' caption='[[3wks]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3wks]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WKS FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wkr|3wkr]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/O-phospho-L-seryl-tRNA:Cys-tRNA_synthase O-phospho-L-seryl-tRNA:Cys-tRNA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.73 2.5.1.73] </span></td></tr>
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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=3wks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wks RCSB], [http://www.ebi.ac.uk/pdbsum/3wks PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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The entry 3wks is ON HOLD until Paper Publication
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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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Authors: Nakazawa, Y., Asano, N., Nakamura, A., Yao, M.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of protein complex
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: O-phospho-L-seryl-tRNA:Cys-tRNA synthase]]
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[[Category: Asano, N.]]
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[[Category: Nakamura, A.]]
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[[Category: Nakazawa, Y.]]
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[[Category: Yao, M.]]
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[[Category: Aminoacyl trna synthesis]]
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[[Category: Transferase]]

Revision as of 07:39, 30 July 2014

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

3wks, resolution 3.03Å

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