1pys
From Proteopedia
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|PDB= 1pys |SIZE=350|CAPTION= <scene name='initialview01'>1pys</scene>, resolution 2.9Å | |PDB= 1pys |SIZE=350|CAPTION= <scene name='initialview01'>1pys</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
- | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pys OCA], [http://www.ebi.ac.uk/pdbsum/1pys PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pys RCSB]</span> | ||
}} | }} | ||
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[[Category: Reshetnikova, L.]] | [[Category: Reshetnikova, L.]] | ||
[[Category: Safro, M.]] | [[Category: Safro, M.]] | ||
- | [[Category: MG]] | ||
[[Category: class ii aminoacyl-trna synthetase]] | [[Category: class ii aminoacyl-trna synthetase]] | ||
[[Category: helix-turn-helix motif]] | [[Category: helix-turn-helix motif]] | ||
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[[Category: thermus thermophilus]] | [[Category: thermus thermophilus]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:28 2008'' |
Revision as of 20:06, 30 March 2008
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, resolution 2.9Å | |||||||
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Ligands: | |||||||
Activity: | Phenylalanine--tRNA ligase, with EC number 6.1.1.20 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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