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1pys
From Proteopedia
(New page: 200px<br /><applet load="1pys" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pys, resolution 2.9Å" /> '''PHENYLALANYL-TRNA SYN...) |
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| - | [[Image:1pys.jpg|left|200px]]<br /><applet load="1pys" size=" | + | [[Image:1pys.jpg|left|200px]]<br /><applet load="1pys" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pys, resolution 2.9Å" /> | caption="1pys, resolution 2.9Å" /> | ||
'''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''<br /> | '''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of phenylalanyl-tRNA synthetase from Thermus | + | The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1PYS 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 MG as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1PYS 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=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1PYS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thermus thermophilus]] | [[Category: thermus thermophilus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:02 2008'' |
Revision as of 12:34, 21 February 2008
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PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
Overview
The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes.
About this Structure
1PYS is a Protein complex structure of sequences from Thermus thermophilus with as ligand. Active as Phenylalanine--tRNA ligase, with EC number 6.1.1.20 Full crystallographic information is available from OCA.
Reference
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus., Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG, Nat Struct Biol. 1995 Jul;2(7):537-47. PMID:7664121
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