1vfg

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|PDB= 1vfg |SIZE=350|CAPTION= <scene name='initialview01'>1vfg</scene>, resolution 2.8&Aring;
|PDB= 1vfg |SIZE=350|CAPTION= <scene name='initialview01'>1vfg</scene>, resolution 2.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER'>APC</scene>
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1miw|1MIW]], [[1ou5|1OU5]], [[1uet|1UET]], [[1r89|1R89]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vfg OCA], [http://www.ebi.ac.uk/pdbsum/1vfg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vfg RCSB]</span>
}}
}}
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[[Category: Ueda, T.]]
[[Category: Ueda, T.]]
[[Category: Vassylyev, D G.]]
[[Category: Vassylyev, D G.]]
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[[Category: APC]]
 
[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rna]]
[[Category: rna]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:44:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:23:37 2008''

Revision as of 21:23, 30 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
Related: 1MIW, 1OU5, 1UET, 1R89


Resources: FirstGlance, OCA, PDBsum, RCSB
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

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