2z2u

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(New page: 200px<br /><applet load="2z2u" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z2u, resolution 2.40&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17727881 17727881]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17727881 17727881]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: metal binding protein]]
[[Category: metal binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:04:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:59:44 2008''

Revision as of 16:59, 21 February 2008


2z2u, resolution 2.40Å

Drag the structure with the mouse to rotate

Crystal structure of archaeal TYW1

Overview

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.

About this Structure

2Z2U is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

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

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