1wxx

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|PDB= 1wxx |SIZE=350|CAPTION= <scene name='initialview01'>1wxx</scene>, resolution 1.80&Aring;
|PDB= 1wxx |SIZE=350|CAPTION= <scene name='initialview01'>1wxx</scene>, resolution 1.80&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1wxw|1WXW]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wxx OCA], [http://www.ebi.ac.uk/pdbsum/1wxx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wxx RCSB]</span>
}}
}}
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[[Category: Shirouzu, M.]]
[[Category: Shirouzu, M.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: K]]
 
-
[[Category: PO4]]
 
[[Category: adomet]]
[[Category: adomet]]
[[Category: methyltransferase]]
[[Category: methyltransferase]]
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[[Category: thermus thermophillus]]
[[Category: thermus thermophillus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:02:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:42:25 2008''

Revision as of 21:42, 30 March 2008

Image:1wxx.gif


PDB ID 1wxx

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: , ,
Related: 1WXW


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Tt1595, a putative SAM-dependent methyltransferase from Thermus thermophillus HB8


Overview

The Thermus thermophilus hypothetical protein TTHA1280 belongs to a family of predicted S-adenosyl-L-methionine (AdoMet) dependent RNA methyltransferases (MTases) present in many bacterial and archaeal species. Inspection of amino-acid sequence motifs common to class I Rossmann-fold-like MTases suggested a specific role as an RNA 5-methyluridine MTase. Selenomethionine (SeMet) labelled and native versions of the protein were expressed, purified and crystallized. Two crystal forms of the SeMet-labelled apoprotein were obtained: SeMet-ApoI and SeMet-ApoII. Cocrystallization of the native protein with S-adenosyl-L-homocysteine (AdoHcy) yielded a third crystal form, Native-AdoHcy. The SeMet-ApoI structure was solved by the multiple anomalous dispersion method and refined at 2.55 A resolution. The SeMet-ApoII and Native-AdoHcy structures were solved by molecular replacement and refined at 1.80 and 2.60 A, respectively. TTHA1280 formed a homodimer in the crystals and in solution. Each subunit folds into a three-domain structure composed of a small N-terminal PUA domain, a central alpha/beta-domain and a C-terminal Rossmann-fold-like MTase domain. The three domains form an overall clamp-like shape, with the putative active site facing a deep cleft. The architecture of the active site is consistent with specific recognition of uridine and catalysis of methyl transfer to the 5-carbon position. The cleft is suitable in size and charge distribution for binding single-stranded RNA.

About this Structure

1WXX is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structures of a putative RNA 5-methyluridine methyltransferase, Thermus thermophilus TTHA1280, and its complex with S-adenosyl-L-homocysteine., Pioszak AA, Murayama K, Nakagawa N, Ebihara A, Kuramitsu S, Shirouzu M, Yokoyama S, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Oct 1;61(Pt, 10):867-74. Epub 2005 Sep 30. PMID:16511182

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