2yy8: Difference between revisions
New page: left|200px {{Structure |PDB= 2yy8 |SIZE=350|CAPTION= <scene name='initialview01'>2yy8</scene>, resolution 2.48Å |SITE= <scene name='pdbsite=AC1:Sam+Binding+Site+... |
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|PDB= 2yy8 |SIZE=350|CAPTION= <scene name='initialview01'>2yy8</scene>, resolution 2.48Å | |PDB= 2yy8 |SIZE=350|CAPTION= <scene name='initialview01'>2yy8</scene>, resolution 2.48Å | ||
|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> | ||
|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> and <scene name='pdbligand=MTA:5 | |LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> and <scene name='pdbligand=MTA:5'-DEOXY-5'-METHYLTHIOADENOSINE'>MTA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:55:47 2008'' | ||
Revision as of 16:55, 23 March 2008
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Crystal structure of archaeal tRNA-methylase for position 56 (aTrm56) from Pyrococcus horikoshii, complexed with S-adenosyl-L-methionine
OverviewOverview
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 StructureAbout this Structure
2YY8 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
ReferenceReference
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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Pyrococcus horikoshii
- Single protein
- Kuratani, M.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Yokoyama, S.
- MTA
- SAM
- Deep trefoil knot
- National project on protein structural and functional analyse
- Nppsfa
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic
- Transferase