1pyb: Difference between revisions

Revision as of 15:33, 21 February 2008

Crystal Structure of Aquifex aeolicus Trbp111: a Stucture-Specific tRNA Binding Protein

OverviewOverview

Trbp111 is a 111 amino acid Aquifex aeolicus structure-specific tRNA-binding protein that has homologous counterparts distributed throughout evolution. A dimer is the functional unit for binding a single tRNA. Here we report the 3D structures of the A.aeolicus protein and its Escherichia coli homolog at resolutions of 2.50 and 1.87 A, respectively. The structure shows a symmetrical dimer of two core domains and a central dimerization domain where the N- and C-terminal regions of Trbp111 form an extensive dimer interface. The core of the monomer is a classical oligonucleotide/oligosaccharide-binding (OB) fold with a five-stranded ss-barrel and a small capping helix. This structure is similar to that seen in the anticodon-binding domain of three class II tRNA synthetases and several other proteins. Mutational analysis identified sites important for interactions with tRNA. These residues line the inner surfaces of two clefts formed between the ss-barrel of each monomer and the dimer interface. The results are consistent with a proposed model for asymmetrical docking of the convex side of tRNA to the dimer.

About this StructureAbout this Structure

1PYB is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of trbp111: a structure-specific tRNA-binding protein., Swairjo MA, Morales AJ, Wang CC, Ortiz AR, Schimmel P, EMBO J. 2000 Dec 1;19(23):6287-98. PMID:11101501

Page seeded by OCA on Thu Feb 21 14:33:50 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1pyb.jpg|left|200px]]<br /><applet load="1pyb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pyb.jpg|left|200px]]<br /><applet load="1pyb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pyb, resolution 2.5&Aring;" />
 '''Crystal Structure of Aquifex aeolicus Trbp111: a Stucture-Specific tRNA Binding Protein'''<br />
 ==Overview==
-Trbp111 is a 111 amino acid Aquifex aeolicus structure-specific, tRNA-binding protein that has homologous counterparts distributed, throughout evolution. A dimer is the functional unit for binding a single, tRNA. Here we report the 3D structures of the A.aeolicus protein and its, Escherichia coli homolog at resolutions of 2.50 and 1.87 A, respectively., The structure shows a symmetrical dimer of two core domains and a central, dimerization domain where the N- and C-terminal regions of Trbp111 form an, extensive dimer interface. The core of the monomer is a classical, oligonucleotide/oligosaccharide-binding (OB) fold with a five-stranded, ss-barrel and a small capping helix. This structure is similar to that, seen in the anticodon-binding domain of three class II tRNA synthetases, and several other proteins. Mutational analysis identified sites important, for interactions with tRNA. These residues line the inner surfaces of two, clefts formed between the ss-barrel of each monomer and the dimer, interface. The results are consistent with a proposed model for, asymmetrical docking of the convex side of tRNA to the dimer.
+Trbp111 is a 111 amino acid Aquifex aeolicus structure-specific tRNA-binding protein that has homologous counterparts distributed throughout evolution. A dimer is the functional unit for binding a single tRNA. Here we report the 3D structures of the A.aeolicus protein and its Escherichia coli homolog at resolutions of 2.50 and 1.87 A, respectively. The structure shows a symmetrical dimer of two core domains and a central dimerization domain where the N- and C-terminal regions of Trbp111 form an extensive dimer interface. The core of the monomer is a classical oligonucleotide/oligosaccharide-binding (OB) fold with a five-stranded ss-barrel and a small capping helix. This structure is similar to that seen in the anticodon-binding domain of three class II tRNA synthetases and several other proteins. Mutational analysis identified sites important for interactions with tRNA. These residues line the inner surfaces of two clefts formed between the ss-barrel of each monomer and the dimer interface. The results are consistent with a proposed model for asymmetrical docking of the convex side of tRNA to the dimer.
 ==About this Structure==
-PYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PYB OCA].
+PYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYB OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Aquifex aeolicus]]
 [[Category: Single protein]]
-[[Category: Morales, A.J.]]
+[[Category: Morales, A J.]]
-[[Category: Ortiz, A.R.]]
+[[Category: Ortiz, A R.]]
 [[Category: Schimmel, P.]]
-[[Category: Swairjo, M.A.]]
+[[Category: Swairjo, M A.]]
-[[Category: Wang, C.C.]]
+[[Category: Wang, C C.]]
 [[Category: beta-barrel]]
 [[Category: ob-fold]]
@@ Line 23: / Line 23: @@
 [[Category: oligosaccharide-binding fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:12:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:50 2008''