2akw

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[[Image:2akw.gif|left|200px]]<br /><applet load="2akw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2akw.gif|left|200px]]
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caption="2akw, resolution 2.800&Aring;" />
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'''Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with p-Cl-Phenylalanine'''<br />
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{{Structure
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|PDB= 2akw |SIZE=350|CAPTION= <scene name='initialview01'>2akw</scene>, resolution 2.800&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=200:4-CHLORO-L-PHENYLALANINE'>200</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20]
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|GENE=
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}}
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'''Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with p-Cl-Phenylalanine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AKW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=200:'>200</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKW OCA].
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2AKW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKW OCA].
==Reference==
==Reference==
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Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase., Kotik-Kogan O, Moor N, Tworowski D, Safro M, Structure. 2005 Dec;13(12):1799-807. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16338408 16338408]
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Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase., Kotik-Kogan O, Moor N, Tworowski D, Safro M, Structure. 2005 Dec;13(12):1799-807. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16338408 16338408]
[[Category: Phenylalanine--tRNA ligase]]
[[Category: Phenylalanine--tRNA ligase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: protein-unnatural amino acid complex]]
[[Category: protein-unnatural amino acid complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:50:51 2008''

Revision as of 13:50, 20 March 2008


PDB ID 2akw

Drag the structure with the mouse to rotate
, resolution 2.800Å
Ligands: , and
Activity: Phenylalanine--tRNA ligase, with EC number 6.1.1.20
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with p-Cl-Phenylalanine


Overview

Aminoacyl-tRNA synthetases (aaRSs) exert control over the faithful transfer of amino acids onto cognate tRNAs. Since chemical structures of various amino acids closely resemble each other, it is difficult to discriminate between them. Editing activity has been evolved by certain aaRSs to resolve the problem. In this study, we determined the crystal structures of complexes of T. thermophilus phenylalanyl-tRNA synthetase (PheRS) with L-tyrosine, p-chloro-phenylalanine, and a nonhydrolyzable tyrosyl-adenylate analog. The structures demonstrate plasticity of the synthetic site capable of binding substrates larger than phenylalanine and provide a structural basis for the proofreading mechanism. The editing site is localized at the B3/B4 interface, 35 A from the synthetic site. Glubeta334 plays a crucial role in the specific recognition of the Tyr moiety in the editing site. The tyrosyl-adenylate analog binds exclusively in the synthetic site. Both structural data and tyrosine-dependent ATP hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential posttransfer editing pathway in the phenylalanine-specific system.

About this Structure

2AKW is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase., Kotik-Kogan O, Moor N, Tworowski D, Safro M, Structure. 2005 Dec;13(12):1799-807. PMID:16338408

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