2z2u

<table><tr><td colspan='2'>[[2z2u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Z2U FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2z2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2u OCA], [http://pdbe.org/2z2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z2u RCSB], [http://www.ebi.ac.uk/pdbsum/2z2u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z2u ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TYW1_METJA TYW1_METJA]] Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).[HAMAP-Rule:MF_01921]<ref>PMID:22026549</ref>

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== Publication Abstract from PubMed ==

Wyosine and its derivatives, such as wybutosine, found in eukaryotic and archaeal tRNAs, are tricyclic hypermodified nucleosides. In eukaryotes, wybutosine exists exclusively in position 37, 3'-adjacent to the anticodon, of tRNA(Phe), where it ensures correct translation by stabilizing the codon-anticodon base-pairing during the ribosomal decoding process. Recent studies revealed that the wyosine biosynthetic pathway consists of multistep enzymatic reactions starting from a guanosine residue. Among these steps, TYW1 catalyzes the second step to form the tricyclic ring structure, by cyclizing N(1)-methylguanosine. In this study, we solved the crystal structure of TYW1 from Methanocaldococcus jannaschii at 2.4 A resolution. TYW1 assumes an incomplete TIM barrel with (alpha/beta)(6) topology, which closely resembles the reported structures of radical SAM enzymes. Hence, TYW1 was considered to catalyze the cyclization reaction by utilizing the radical intermediate. Comparison with other radical SAM enzymes allowed us to build a model structure complexed with S-adenosylmethionine and two [4Fe-4S] clusters. Mutational analyses in yeast supported the validity of this complex model structure, which provides a structural insight into the radical reaction involving two [4Fe-4S] clusters to create a complex tricyclic base.

Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA.,Suzuki Y, Noma A, Suzuki T, Senda M, Senda T, Ishitani R, Nureki O J Mol Biol. 2007 Oct 5;372(5):1204-14. Epub 2007 Jul 26. PMID:17727881<ref>PMID:17727881</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2z2u" style="background-color:#fffaf0;"></div>

[[Category: Atcc 43067]]

[[Category: Ishitani, R]]

[[Category: Nureki, O]]

[[Category: Suzuki, Y]]

[[Category: Metal binding protein]]