1wwr: Difference between revisions

Revision as of 16:48, 21 February 2008

Crystal structure of tRNA adenosine deaminase TadA from Aquifex aeolicus

OverviewOverview

The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the adenosine residue at the wobble position of tRNA(Arg-2). This modification is essential for the decoding system. In this study, we determined the crystal structure of Aquifex aeolicus TadA at a 1.8-A resolution. This is the first structure of a deaminase acting on tRNA. A. aeolicus TadA has an alpha/beta/alpha three-layered fold and forms a homodimer. The A. aeolicus TadA dimeric structure is completely different from the tetrameric structure of yeast CDD1, which deaminates mRNA and cytidine, but is similar to the dimeric structure of yeast cytosine deaminase. However, in the A. aeolicus TadA structure, the shapes of the C-terminal helix and the regions between the beta4 and beta5 strands are quite distinct from those of yeast cytosine deaminase and a large cavity is produced. This cavity contains many conserved amino acid residues that are likely to be involved in either catalysis or tRNA binding. We made a docking model of TadA with the tRNA anticodon stem loop.

About this StructureAbout this Structure

1WWR is a Single protein structure of sequence from Aquifex aeolicus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus., Kuratani M, Ishii R, Bessho Y, Fukunaga R, Sengoku T, Shirouzu M, Sekine S, Yokoyama S, J Biol Chem. 2005 Apr 22;280(16):16002-8. Epub 2005 Jan 26. PMID:15677468

Page seeded by OCA on Thu Feb 21 15:48:51 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1wwr.gif|left|200px]]<br /><applet load="1wwr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1wwr.gif|left|200px]]<br /><applet load="1wwr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1wwr, resolution 1.80&Aring;" />
 '''Crystal structure of tRNA adenosine deaminase TadA from Aquifex aeolicus'''<br />
 ==Overview==
-The bacterial tRNA adenosine deaminase (TadA) generates inosine by, deaminating the adenosine residue at the wobble position of tRNA(Arg-2)., This modification is essential for the decoding system. In this study, we, determined the crystal structure of Aquifex aeolicus TadA at a 1.8-A, resolution. This is the first structure of a deaminase acting on tRNA. A., aeolicus TadA has an alpha/beta/alpha three-layered fold and forms a, homodimer. The A. aeolicus TadA dimeric structure is completely different, from the tetrameric structure of yeast CDD1, which deaminates mRNA and, cytidine, but is similar to the dimeric structure of yeast cytosine, deaminase. However, in the A. aeolicus TadA structure, the shapes of the, C-terminal helix and the regions between the beta4 and beta5 strands are, quite distinct from those of yeast cytosine deaminase and a large cavity, is produced. This cavity contains many conserved amino acid residues that, are likely to be involved in either catalysis or tRNA binding. We made a, docking model of TadA with the tRNA anticodon stem loop.
+The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the adenosine residue at the wobble position of tRNA(Arg-2). This modification is essential for the decoding system. In this study, we determined the crystal structure of Aquifex aeolicus TadA at a 1.8-A resolution. This is the first structure of a deaminase acting on tRNA. A. aeolicus TadA has an alpha/beta/alpha three-layered fold and forms a homodimer. The A. aeolicus TadA dimeric structure is completely different from the tetrameric structure of yeast CDD1, which deaminates mRNA and cytidine, but is similar to the dimeric structure of yeast cytosine deaminase. However, in the A. aeolicus TadA structure, the shapes of the C-terminal helix and the regions between the beta4 and beta5 strands are quite distinct from those of yeast cytosine deaminase and a large cavity is produced. This cavity contains many conserved amino acid residues that are likely to be involved in either catalysis or tRNA binding. We made a docking model of TadA with the tRNA anticodon stem loop.
 ==About this Structure==
-WWR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WWR OCA].
+WWR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WWR OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: Ishii, R.]]
 [[Category: Kuratani, M.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Sekine, S.]]
 [[Category: Sengoku, T.]]
@@ Line 27: / Line 27: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:43:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:51 2008''