1jzq

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[[Image:1jzq.gif|left|200px]]<br /><applet load="1jzq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jzq.gif|left|200px]]
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caption="1jzq, resolution 3.0&Aring;" />
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'''Isoleucyl-tRNA synthetase Complexed with Isoleucyl-adenylate analogue'''<br />
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{{Structure
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|PDB= 1jzq |SIZE=350|CAPTION= <scene name='initialview01'>1jzq</scene>, resolution 3.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ILA:N-[ISOLEUCINYL]-N'-[ADENOSYL]-DIAMINOSUFONE'>ILA</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Isoleucyl-tRNA synthetase Complexed with Isoleucyl-adenylate analogue'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JZQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ILA:'>ILA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1JZQ OCA].
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1JZQ is a [[Single protein]] structure of sequence 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=1JZQ OCA].
==Reference==
==Reference==
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Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase., Nakama T, Nureki O, Yokoyama S, J Biol Chem. 2001 Dec 14;276(50):47387-93. Epub 2001 Oct 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11584022 11584022]
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Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase., Nakama T, Nureki O, Yokoyama S, J Biol Chem. 2001 Dec 14;276(50):47387-93. Epub 2001 Oct 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11584022 11584022]
[[Category: Isoleucine--tRNA ligase]]
[[Category: Isoleucine--tRNA ligase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:10:39 2008''

Revision as of 10:10, 20 March 2008


PDB ID 1jzq

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands: and
Activity: Isoleucine--tRNA ligase, with EC number 6.1.1.5
Coordinates: save as pdb, mmCIF, xml



Isoleucyl-tRNA synthetase Complexed with Isoleucyl-adenylate analogue


Overview

An analogue of isoleucyl-adenylate (Ile-AMS) potently inhibits the isoleucyl-tRNA synthetases (IleRSs) from the three primary kingdoms, whereas the antibiotic mupirocin inhibits only the eubacterial and archaeal IleRSs, but not the eukaryotic enzymes, and therefore is clinically used against methicillin-resistant Staphylococcus aureus. We determined the crystal structures of the IleRS from the thermophilic eubacterium, Thermus thermophilus, in complexes with Ile-AMS and mupirocin at 3.0- and 2.5-A resolutions, respectively. A structural comparison of the IleRS.Ile-AMS complex with the adenylate complexes of other aminoacyl-tRNA synthetases revealed the common recognition mode of aminoacyl-adenylate by the class I aminoacyl-tRNA synthetases. The Ile-AMS and mupirocin, which have significantly different chemical structures, are recognized by many of the same amino acid residues of the IleRS, suggesting that the antibiotic inhibits the enzymatic activity by blocking the binding site of the high energy intermediate, Ile-AMP. In contrast, the two amino acid residues that concomitantly recognize Ile-AMS and mupirocin are different between the eubacterial/archaeal IleRSs and the eukaryotic IleRSs. Mutagenic analyses revealed that the replacement of the two residues significantly changed the sensitivity to mupirocin.

About this Structure

1JZQ is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase., Nakama T, Nureki O, Yokoyama S, J Biol Chem. 2001 Dec 14;276(50):47387-93. Epub 2001 Oct 2. PMID:11584022

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