1nyl: Difference between revisions
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[[Image:1nyl.jpg|left|200px]] | [[Image:1nyl.jpg|left|200px]] | ||
'''Unliganded glutaminyl-tRNA synthetase''' | {{Structure | ||
|PDB= 1nyl |SIZE=350|CAPTION= <scene name='initialview01'>1nyl</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] | |||
|GENE= glnS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Unliganded glutaminyl-tRNA synthetase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NYL is a [ | 1NYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYL OCA]. | ||
==Reference== | ==Reference== | ||
tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase., Sherlin LD, Perona JJ, Structure. 2003 May;11(5):591-603. PMID:[http:// | tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase., Sherlin LD, Perona JJ, Structure. 2003 May;11(5):591-603. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12737824 12737824] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Glutamine--tRNA ligase]] | [[Category: Glutamine--tRNA ligase]] | ||
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[[Category: ligase]] | [[Category: ligase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:03:29 2008'' |
Revision as of 14:03, 20 March 2008
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, resolution 2.60Å | |||||||
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Gene: | glnS (Escherichia coli) | ||||||
Activity: | Glutamine--tRNA ligase, with EC number 6.1.1.18 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Unliganded glutaminyl-tRNA synthetase
OverviewOverview
The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase (GlnRS) at 2.4 A resolution shows that substrate binding is essential to construction of a catalytically proficient active site. tRNA binding generates structural changes throughout the enzyme, repositioning key active site peptides that bind glutamine and ATP. The structure gives insight into longstanding questions regarding the tRNA dependence of glutaminyl adenylate formation, the coupling of amino acid and tRNA selectivities, and the roles of specific pathways for transmission of tRNA binding signals to the active site. Comparative analysis of the unliganded and tRNA-bound structures shows, in detail, how flexibility is built into the enzyme architecture and suggests that the induced-fit transitions are a key underlying determinant of both amino acid and tRNA specificity.
About this StructureAbout this Structure
1NYL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase., Sherlin LD, Perona JJ, Structure. 2003 May;11(5):591-603. PMID:12737824
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