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4-Demethylwyosine S...
4-Demethylwyosine Synthase from Pyrococcus abyssi Is a Radical-S-adenosyl-l-methionine Enzyme with an Additional [4Fe-4S]+2 Cluster That Interacts with the Pyruvate Co-substrate
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Perche-Letuvée, Phanélie (författare)
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Kathirvelu, Velavan (författare)
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Berggren, Gustav (författare)
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Clemancey, Martin (författare)
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Latour, Jean-Marc (författare)
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Maurel, Vincent (författare)
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Douki, Thierry (författare)
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Armengaud, Jean (författare)
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Mulliez, Etienne (författare)
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Fontecave, Marc (författare)
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Garcia-Serres, Ricardo (författare)
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Gambarelli, Serge (författare)
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Atta, Mohamed (författare)
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- 2012
- 2012
- Engelska.
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Ingår i: Journal of Biological Chemistry. ; 287:49, s. 41174-41185
- Relaterad länk:
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http://www.jbc.org/c...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- Wybutosine and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the decoding function of the ribosome. The second step in the biosynthesis of wybutosine is catalyzed by TYW1 protein, which is a member of the well established class of metalloenzymes called “Radical-SAM.” These enzymes use a [4Fe-4S] cluster, chelated by three cysteines in a CX3CX2C motif, and S-adenosyl-l-methionine (SAM) to generate a 5′-deoxyadenosyl radical that initiates various chemically challenging reactions. Sequence analysis of TYW1 proteins revealed, in the N-terminal half of the enzyme beside the Radical-SAM cysteine triad, an additional highly conserved cysteine motif. In this study we show by combining analytical and spectroscopic methods including UV-visible absorption, Mössbauer, EPR, and HYSCORE spectroscopies that these additional cysteines are involved in the coordination of a second [4Fe-4S] cluster displaying a free coordination site that interacts with pyruvate, the second substrate of the reaction. The presence of two distinct iron-sulfur clusters on TYW1 is reminiscent of MiaB, another tRNA-modifying metalloenzyme whose active form was shown to bind two iron-sulfur clusters. A possible role for the second [4Fe-4S] cluster in the enzyme activity is discussed.
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Perche-Letuvée, ...
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Kathirvelu, Vela ...
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Berggren, Gustav
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Clemancey, Marti ...
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Latour, Jean-Mar ...
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Maurel, Vincent
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visa fler...
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Douki, Thierry
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Armengaud, Jean
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Mulliez, Etienne
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Fontecave, Marc
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Garcia-Serres, R ...
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Gambarelli, Serg ...
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Atta, Mohamed
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visa färre...
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- Journal of Biolo ...
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Uppsala universitet