1wxw: Difference between revisions
New page: left|200px<br /><applet load="1wxw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wxw, resolution 2.55Å" /> '''Crystal structure of... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1wxw.gif|left|200px]]<br /><applet load="1wxw" size=" | [[Image:1wxw.gif|left|200px]]<br /><applet load="1wxw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1wxw, resolution 2.55Å" /> | caption="1wxw, resolution 2.55Å" /> | ||
'''Crystal structure of Tt1595, a putative SAM-dependent methyltransferase from Thermus thermophillus HB8'''<br /> | '''Crystal structure of Tt1595, a putative SAM-dependent methyltransferase from Thermus thermophillus HB8'''<br /> | ||
==Overview== | ==Overview== | ||
The Thermus thermophilus hypothetical protein TTHA1280 belongs to a family | 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== | ==About this Structure== | ||
1WXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with HEZ as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1WXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=HEZ:'>HEZ</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WXW OCA]. | ||
==Reference== | ==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 | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511182 16511182] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
| Line 17: | Line 17: | ||
[[Category: Murayama, K.]] | [[Category: Murayama, K.]] | ||
[[Category: Nakagawa, N.]] | [[Category: Nakagawa, N.]] | ||
[[Category: Pioszak, A | [[Category: Pioszak, A A.]] | ||
[[Category: RSGI, RIKEN | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| Line 31: | Line 31: | ||
[[Category: thermus thermophillus]] | [[Category: thermus thermophillus]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:13 2008'' | ||
Revision as of 13:49, 21 February 2008
|
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
1WXW is a Single protein structure of sequence from Thermus thermophilus with HEZ as ligand. 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
Page seeded by OCA on Thu Feb 21 15:49:13 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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.
- HEZ
- Adomet
- Methyltransferase
- National project on protein structural and functional analyses
- Nppsfa
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomics
- Thermus thermophillus
