1j2b

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(New page: 200px<br /><applet load="1j2b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j2b, resolution 3.30&Aring;" /> '''Crystal Structure Of...)
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[[Image:1j2b.gif|left|200px]]<br /><applet load="1j2b" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j2b.gif|left|200px]]<br /><applet load="1j2b" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1j2b, resolution 3.30&Aring;" />
caption="1j2b, resolution 3.30&Aring;" />
'''Crystal Structure Of Archaeosine tRNA-Guanine Transglycosylase Complexed With lambda-form tRNA(Val)'''<br />
'''Crystal Structure Of Archaeosine tRNA-Guanine Transglycosylase Complexed With lambda-form tRNA(Val)'''<br />
==Overview==
==Overview==
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Transfer RNA (tRNA) canonically has the clover-leaf secondary structure, with the acceptor, D, anticodon, and T arms, which are folded into the, L-shaped tertiary structure. To strengthen the L form, posttranscriptional, modifications occur on nucleotides buried within the core, but the, modification enzymes are paradoxically inaccessible to them in the L form., In this study, we determined the crystal structure of tRNA bound with, archaeosine tRNA-guanine transglycosylase, which modifies G15 of the D arm, in the core. The bound tRNA assumes an alternative conformation ("lambda, form") drastically different from the L form. All of the D-arm secondary, base pairs and the canonical tertiary interactions are disrupted., Furthermore, a helical structure is reorganized, while the rest of the D, arm is single stranded and protruded. Consequently, the enzyme precisely, locates the exposed G15 in the active site, by counting the nucleotide, number from G1 to G15 in the lambda form.
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Transfer RNA (tRNA) canonically has the clover-leaf secondary structure with the acceptor, D, anticodon, and T arms, which are folded into the L-shaped tertiary structure. To strengthen the L form, posttranscriptional modifications occur on nucleotides buried within the core, but the modification enzymes are paradoxically inaccessible to them in the L form. In this study, we determined the crystal structure of tRNA bound with archaeosine tRNA-guanine transglycosylase, which modifies G15 of the D arm in the core. The bound tRNA assumes an alternative conformation ("lambda form") drastically different from the L form. All of the D-arm secondary base pairs and the canonical tertiary interactions are disrupted. Furthermore, a helical structure is reorganized, while the rest of the D arm is single stranded and protruded. Consequently, the enzyme precisely locates the exposed G15 in the active site, by counting the nucleotide number from G1 to G15 in the lambda form.
==About this Structure==
==About this Structure==
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1J2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with ZN and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Queuine_tRNA-ribosyltransferase Queuine tRNA-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.29 2.4.2.29] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J2B OCA].
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1J2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Queuine_tRNA-ribosyltransferase Queuine tRNA-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.29 2.4.2.29] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2B OCA].
==Reference==
==Reference==
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[[Category: Nureki, O.]]
[[Category: Nureki, O.]]
[[Category: Okada, N.]]
[[Category: Okada, N.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:52:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:09 2008''

Revision as of 11:18, 21 February 2008


1j2b, resolution 3.30Å

Drag the structure with the mouse to rotate

Crystal Structure Of Archaeosine tRNA-Guanine Transglycosylase Complexed With lambda-form tRNA(Val)

Overview

Transfer RNA (tRNA) canonically has the clover-leaf secondary structure with the acceptor, D, anticodon, and T arms, which are folded into the L-shaped tertiary structure. To strengthen the L form, posttranscriptional modifications occur on nucleotides buried within the core, but the modification enzymes are paradoxically inaccessible to them in the L form. In this study, we determined the crystal structure of tRNA bound with archaeosine tRNA-guanine transglycosylase, which modifies G15 of the D arm in the core. The bound tRNA assumes an alternative conformation ("lambda form") drastically different from the L form. All of the D-arm secondary base pairs and the canonical tertiary interactions are disrupted. Furthermore, a helical structure is reorganized, while the rest of the D arm is single stranded and protruded. Consequently, the enzyme precisely locates the exposed G15 in the active site, by counting the nucleotide number from G1 to G15 in the lambda form.

About this Structure

1J2B is a Single protein structure of sequence from Pyrococcus horikoshii with and as ligands. Active as Queuine tRNA-ribosyltransferase, with EC number 2.4.2.29 Full crystallographic information is available from OCA.

Reference

Alternative tertiary structure of tRNA for recognition by a posttranscriptional modification enzyme., Ishitani R, Nureki O, Nameki N, Okada N, Nishimura S, Yokoyama S, Cell. 2003 May 2;113(3):383-94. PMID:12732145

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