1wxx
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(New page: 200px<br /><applet load="1wxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wxx, resolution 1.80Å" /> '''Crystal structure of...)
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Revision as of 22:53, 24 November 2007
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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 with K and PO4 as ligands. 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 Crystallograph Sect F Struct Biol Cryst Commun. 2005 Oct 1;61(Pt, 10):867-74. Epub 2005 Sep 30. PMID:16511182
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Categories: Single protein | Thermus thermophilus | Ebihara, A. | Kuramitsu, S. | Murayama, K. | Nakagawa, N. | Pioszak, A.A. | RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative. | Shirouzu, M. | Yokoyama, S. | K | PO4 | Adomet | Methyltransferase | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | Thermus thermophillus