1wy5

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[[Image:1wy5.gif|left|200px]]<br /><applet load="1wy5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wy5.gif|left|200px]]
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caption="1wy5, resolution 2.42&Aring;" />
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'''Crystal structure of isoluecyl-tRNA lysidine synthetase'''<br />
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{{Structure
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|PDB= 1wy5 |SIZE=350|CAPTION= <scene name='initialview01'>1wy5</scene>, resolution 2.42&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of isoluecyl-tRNA lysidine synthetase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1WY5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WY5 OCA].
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1WY5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WY5 OCA].
==Reference==
==Reference==
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Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain., Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7487-92. Epub 2005 May 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15894617 15894617]
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Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain., Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7487-92. Epub 2005 May 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15894617 15894617]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Suzuki, T.]]
[[Category: Suzuki, T.]]
[[Category: n-type atp-ppase]]
[[Category: n-type atp-ppase]]
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[[Category: national project on protein structural and functional analyses]]
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[[Category: national project on protein structural and functional analyse]]
[[Category: nppsfa]]
[[Category: nppsfa]]
[[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]]
[[Category: translation]]
[[Category: translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:02:57 2008''

Revision as of 13:02, 20 March 2008


PDB ID 1wy5

Drag the structure with the mouse to rotate
, resolution 2.42Å
Coordinates: save as pdb, mmCIF, xml



Crystal structure of isoluecyl-tRNA lysidine synthetase


Overview

Lysidine, a lysine-combined modified cytidine, is exclusively located at the anticodon wobble position (position 34) of eubacterial tRNA(Ile)(2) and not only converts the codon specificity from AUG to AUA, but also converts the aminoacylation specificity from recognition by methionyl-tRNA synthetase to that by isoleucyl-tRNA synthetase (IleRS). Here, we report the crystal structure of lysidine synthetase (TilS) from Aquifex aeolicus at 2.42-A resolution. TilS forms a homodimer, and each subunit consists of the N-terminal dinucleotide-binding fold domain (NTD), with a characteristic central hole, and the C-terminal globular domain (CTD) connected by a long alpha-helical linker. The NTD shares striking structural similarity with the ATP-pyrophosphatase domain of GMP synthetase, which reminds us of the two-step reaction by TilS: adenylation of C34 and lysine attack on the C2 carbon. Conserved amino acid residues are clustered around the NTD central hole. Kinetic analyses of the conserved residues' mutants indicated that C34 of tRNA(Ile)(2) is adenylated by an ATP lying across the NTD central hole and that a lysine, which is activated at a loop appended to the NTD, nucleophilically attacks the C2 carbon from the rear. Escherichia coli TilS (called MesJ) has an additional CTD, which may recognize the tRNA(Ile)(2) acceptor stem. In contrast, a mutational study revealed that A. aeolicus TilS does not recognize the tRNA acceptor stem but recognizes the C29.G41 base pair in the anticodon stem. Thus, the two TilS enzymes discriminate tRNA(Ile)(2) from tRNA(Met) by strategies similar to that used by IleRS, but in distinct manners.

About this Structure

1WY5 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain., Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7487-92. Epub 2005 May 13. PMID:15894617

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