1ffy: Difference between revisions

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New page: left|200px<br /> <applet load="1ffy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ffy, resolution 2.2Å" /> '''INSIGHTS INTO EDITIN...
 
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[[Image:1ffy.gif|left|200px]]<br />
[[Image:1ffy.gif|left|200px]]<br /><applet load="1ffy" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1ffy" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1ffy, resolution 2.2&Aring;" />
caption="1ffy, resolution 2.2&Aring;" />
'''INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN'''<br />
'''INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN'''<br />


==Overview==
==Overview==
Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at, its synthetic active site and hydrolyzes incorrectly acylated amino acids, at its editing active site. The 2.2 angstrom resolution crystal structure, of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin, shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active, site. To position the 3' terminus in the synthetic active site, the, acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln), complexed with its synthetase. The amino acid editing activity of the, IleRS may result from the incorrect products shuttling between the, synthetic and editing active sites, which is reminiscent of the editing, mechanism of DNA polymerases.
Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes incorrectly acylated amino acids at its editing active site. The 2.2 angstrom resolution crystal structure of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active site. To position the 3' terminus in the synthetic active site, the acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln) complexed with its synthetase. The amino acid editing activity of the IleRS may result from the incorrect products shuttling between the synthetic and editing active sites, which is reminiscent of the editing mechanism of DNA polymerases.


==About this Structure==
==About this Structure==
1FFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with K, ZN, MG and MRC as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1FFY with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Isoleucine--tRNA_ligase Isoleucine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.5 6.1.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FFY OCA].  
1FFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=MRC:'>MRC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1FFY with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Isoleucine--tRNA_ligase Isoleucine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.5 6.1.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFY OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Silvian, L.F.]]
[[Category: Silvian, L F.]]
[[Category: Steitz, T.A.]]
[[Category: Steitz, T A.]]
[[Category: Wang, J.]]
[[Category: Wang, J.]]
[[Category: K]]
[[Category: K]]
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[[Category: staphylococcus aureus]]
[[Category: staphylococcus aureus]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:00:09 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:16 2008''

Revision as of 13:38, 21 February 2008

File:1ffy.gif


1ffy, resolution 2.2Å

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INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN

OverviewOverview

Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes incorrectly acylated amino acids at its editing active site. The 2.2 angstrom resolution crystal structure of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active site. To position the 3' terminus in the synthetic active site, the acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln) complexed with its synthetase. The amino acid editing activity of the IleRS may result from the incorrect products shuttling between the synthetic and editing active sites, which is reminiscent of the editing mechanism of DNA polymerases.

About this StructureAbout this Structure

1FFY is a Single protein structure of sequence from Staphylococcus aureus with , , and as ligands. The following page contains interesting information on the relation of 1FFY with [Aminoacyl-tRNA Synthetases]. Active as Isoleucine--tRNA ligase, with EC number 6.1.1.5 Full crystallographic information is available from OCA.

ReferenceReference

Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin., Silvian LF, Wang J, Steitz TA, Science. 1999 Aug 13;285(5430):1074-7. PMID:10446055

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