2yy8

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(New page: 200px {{Structure |PDB= 2yy8 |SIZE=350|CAPTION= <scene name='initialview01'>2yy8</scene>, resolution 2.48&Aring; |SITE= <scene name='pdbsite=AC1:Sam+Binding+Site+...)
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|PDB= 2yy8 |SIZE=350|CAPTION= <scene name='initialview01'>2yy8</scene>, resolution 2.48&Aring;
|PDB= 2yy8 |SIZE=350|CAPTION= <scene name='initialview01'>2yy8</scene>, resolution 2.48&Aring;
|SITE= <scene name='pdbsite=AC1:Sam+Binding+Site+For+Residue+B+500'>AC1</scene> and <scene name='pdbsite=AC2:Mta+Binding+Site+For+Residue+A+400'>AC2</scene>
|SITE= <scene name='pdbsite=AC1:Sam+Binding+Site+For+Residue+B+500'>AC1</scene> and <scene name='pdbsite=AC2:Mta+Binding+Site+For+Residue+A+400'>AC2</scene>
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|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> and <scene name='pdbligand=MTA:5'-DEOXY-5'-METHYLTHIOADENOSINE'>MTA</scene>
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|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> and <scene name='pdbligand=MTA:5&#39;-DEOXY-5&#39;-METHYLTHIOADENOSINE'>MTA</scene>
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:55:47 2008''

Revision as of 13:55, 23 March 2008

Image:2yy8.jpg


PDB ID 2yy8

Drag the structure with the mouse to rotate
, resolution 2.48Å
Sites: and
Ligands: and
Coordinates: save as pdb, mmCIF, xml



Crystal structure of archaeal tRNA-methylase for position 56 (aTrm56) from Pyrococcus horikoshii, complexed with S-adenosyl-L-methionine


Overview

The conserved cytidine residue at position 56 of tRNA contributes to the maintenance of the L-shaped tertiary structure. aTrm56 catalyzes the 2'-O-methylation of the cytidine residue in archaeal tRNA, using S-adenosyl-L-methionine. Based on the amino acid sequence, aTrm56 is the most distant member of the SpoU family. Here, we determined the crystal structure of Pyrococcus horikoshii aTrm56 complexed with S-adenosyl-L-methionine at 2.48 A resolution. aTrm56 consists of the SPOUT domain, which contains the characteristic deep trefoil knot, and a unique C-terminal beta-hairpin. aTrm56 forms a dimer. The S-adenosyl-L-methionine binding and dimerization of aTrm56 were similar to those of the other SpoU members. A structure-based sequence alignment revealed that aTrm56 conserves only motif II, among the four signature motifs. However, an essential Arg16 residue is located at a novel position within motif I. Biochemical assays showed that aTrm56 prefers the L-shaped tRNA to the lambda form as its substrate.

About this Structure

2YY8 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Crystal structure and mutational study of a unique SpoU family archaeal methylase that forms 2'-O-methylcytidine at position 56 of tRNA., Kuratani M, Bessho Y, Nishimoto M, Grosjean H, Yokoyama S, J Mol Biol. 2008 Jan 25;375(4):1064-75. Epub 2007 Nov 17. PMID:18068186

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