1vfg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vfg.gif|left|200px]]<br /><applet load="1vfg" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1vfg.gif|left|200px]]
-
caption="1vfg, resolution 2.8&Aring;" />
+
 
-
'''Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog'''<br />
+
{{Structure
 +
|PDB= 1vfg |SIZE=350|CAPTION= <scene name='initialview01'>1vfg</scene>, resolution 2.8&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER'>APC</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1VFG 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=APC:'>APC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFG OCA].
+
1VFG is a [[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=1VFG OCA].
==Reference==
==Reference==
-
Structural basis for template-independent RNA polymerization., Tomita K, Fukai S, Ishitani R, Ueda T, Takeuchi N, Vassylyev DG, Nureki O, Nature. 2004 Aug 5;430(7000):700-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15295603 15295603]
+
Structural basis for template-independent RNA polymerization., Tomita K, Fukai S, Ishitani R, Ueda T, Takeuchi N, Vassylyev DG, Nureki O, Nature. 2004 Aug 5;430(7000):700-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15295603 15295603]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Polynucleotide adenylyltransferase]]
[[Category: Polynucleotide adenylyltransferase]]
Line 26: Line 35:
[[Category: rna]]
[[Category: rna]]
[[Category: rsgi]]
[[Category: rsgi]]
-
[[Category: structural genomics]]
+
[[Category: structural genomic]]
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:42 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:44:47 2008''

Revision as of 12:44, 20 March 2008


PDB ID 1vfg

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands:
Activity: Polynucleotide adenylyltransferase, with EC number 2.7.7.19
Coordinates: save as pdb, mmCIF, xml



Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog


Overview

The 3'-terminal CCA nucleotide sequence (positions 74-76) of transfer RNA is essential for amino acid attachment and interaction with the ribosome during protein synthesis. The CCA sequence is synthesized de novo and/or repaired by a template-independent RNA polymerase, 'CCA-adding enzyme', using CTP and ATP as substrates. Despite structural and biochemical studies, the mechanism by which the CCA-adding enzyme synthesizes the defined sequence without a nucleic acid template remains elusive. Here we present the crystal structure of Aquifex aeolicus CCA-adding enzyme, bound to a primer tRNA lacking the terminal adenosine and an incoming ATP analogue, at 2.8 A resolution. The enzyme enfolds the acceptor T helix of the tRNA molecule. In the catalytic pocket, C75 is adjacent to ATP, and their base moieties are stacked. The complementary pocket for recognizing C74-C75 of tRNA forms a 'protein template' for the penultimate two nucleotides, mimicking the nucleotide template used by template-dependent polymerases. These results are supported by systematic analyses of mutants. Our structure represents the 'pre-insertion' stage of selecting the incoming nucleotide and provides the structural basis for the mechanism underlying template-independent RNA polymerization.

About this Structure

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

Reference

Structural basis for template-independent RNA polymerization., Tomita K, Fukai S, Ishitani R, Ueda T, Takeuchi N, Vassylyev DG, Nureki O, Nature. 2004 Aug 5;430(7000):700-4. PMID:15295603

Page seeded by OCA on Thu Mar 20 14:44:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools