2cww: Difference between revisions

No edit summary
No edit summary
Line 1: Line 1:
[[Image:2cww.gif|left|200px]]
{{Seed}}
[[Image:2cww.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cww|  PDB=2cww  |  SCENE=  }}  
{{STRUCTURE_2cww|  PDB=2cww  |  SCENE=  }}  


'''Crystal structure of Thermus thermophilus TTHA1280, a putative SAM-dependent RNA methyltransferase, in complex with S-adenosyl-L-homocysteine'''
===Crystal structure of Thermus thermophilus TTHA1280, a putative SAM-dependent RNA methyltransferase, in complex with S-adenosyl-L-homocysteine===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_16511182}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16511182 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16511182}}


==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Sam-dependent rna methyltransferase]]
[[Category: Sam-dependent rna methyltransferase]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 23:14:42 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:52:21 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA