1p9p
From Proteopedia
(New page: 200px<br /><applet load="1p9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9p, resolution 2.5Å" /> '''The Crystal Structure...) |
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| - | [[Image:1p9p.gif|left|200px]]<br /><applet load="1p9p" size=" | + | [[Image:1p9p.gif|left|200px]]<br /><applet load="1p9p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p9p, resolution 2.5Å" /> | caption="1p9p, resolution 2.5Å" /> | ||
'''The Crystal Structure of a M1G37 tRNA Methyltransferase, TrmD'''<br /> | '''The Crystal Structure of a M1G37 tRNA Methyltransferase, TrmD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Escherichia coli tRNA (guanosine-1) | + | The crystal structure of Escherichia coli tRNA (guanosine-1) methyltransferase (TrmD) complexed with S-adenosyl homocysteine (AdoHcy) has been determined at 2.5A resolution. TrmD, which methylates G37 of tRNAs containing the sequence G36pG37, is a homo-dimer. Each monomer consists of a C-terminal domain connected by a flexible linker to an N-terminal AdoMet-binding domain. The two bound AdoHcy moieties are buried at the bottom of deep clefts. The dimer structure appears integral to the formation of the catalytic center of the enzyme and this arrangement strongly suggests that the anticodon loop of tRNA fits into one of these clefts for methyl transfer to occur. In addition, adjacent hydrophobic sites in the cleft delineate a defined pocket, which may accommodate the GpG sequence during catalysis. The dimer contains two deep trefoil peptide knots and a peptide loop extending from each knot embraces the AdoHcy adenine ring. Mutational analyses demonstrate that the knot is important for AdoMet binding and catalytic activity, and that the C-terminal domain is not only required for tRNA binding but plays a functional role in catalytic activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1P9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_escherichia_coli_o6,_escherichia_coli_o157:h7,_and_shigella_flexneri Escherichia coli, escherichia coli o6, escherichia coli o157:h7, and shigella flexneri] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/tRNA_(guanine-N(1)-)-methyltransferase tRNA (guanine-N(1)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.31 2.1.1.31] Full crystallographic information is available from [http:// | + | 1P9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_escherichia_coli_o6,_escherichia_coli_o157:h7,_and_shigella_flexneri Escherichia coli, escherichia coli o6, escherichia coli o157:h7, and shigella flexneri] with <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/tRNA_(guanine-N(1)-)-methyltransferase tRNA (guanine-N(1)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.31 2.1.1.31] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tRNA (guanine-N(1)-)-methyltransferase]] | [[Category: tRNA (guanine-N(1)-)-methyltransferase]] | ||
[[Category: Andraos-Selim, C.]] | [[Category: Andraos-Selim, C.]] | ||
| - | [[Category: Elkins, P | + | [[Category: Elkins, P A.]] |
| - | [[Category: Holmes, W | + | [[Category: Holmes, W M.]] |
[[Category: Rastinejad, F.]] | [[Category: Rastinejad, F.]] | ||
[[Category: Redlak, M.]] | [[Category: Redlak, M.]] | ||
| - | [[Category: Thiel, A | + | [[Category: Thiel, A Van.]] |
| - | [[Category: Vitaszka, P | + | [[Category: Vitaszka, P R.]] |
| - | [[Category: Watts, J | + | [[Category: Watts, J M.]] |
[[Category: Zalacain, M.]] | [[Category: Zalacain, M.]] | ||
[[Category: SAH]] | [[Category: SAH]] | ||
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[[Category: spout]] | [[Category: spout]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:40 2008'' |
Revision as of 12:26, 21 February 2008
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The Crystal Structure of a M1G37 tRNA Methyltransferase, TrmD
Overview
The crystal structure of Escherichia coli tRNA (guanosine-1) methyltransferase (TrmD) complexed with S-adenosyl homocysteine (AdoHcy) has been determined at 2.5A resolution. TrmD, which methylates G37 of tRNAs containing the sequence G36pG37, is a homo-dimer. Each monomer consists of a C-terminal domain connected by a flexible linker to an N-terminal AdoMet-binding domain. The two bound AdoHcy moieties are buried at the bottom of deep clefts. The dimer structure appears integral to the formation of the catalytic center of the enzyme and this arrangement strongly suggests that the anticodon loop of tRNA fits into one of these clefts for methyl transfer to occur. In addition, adjacent hydrophobic sites in the cleft delineate a defined pocket, which may accommodate the GpG sequence during catalysis. The dimer contains two deep trefoil peptide knots and a peptide loop extending from each knot embraces the AdoHcy adenine ring. Mutational analyses demonstrate that the knot is important for AdoMet binding and catalytic activity, and that the C-terminal domain is not only required for tRNA binding but plays a functional role in catalytic activity.
About this Structure
1P9P is a Single protein structure of sequence from Escherichia coli, escherichia coli o6, escherichia coli o157:h7, and shigella flexneri with as ligand. Active as tRNA (guanine-N(1)-)-methyltransferase, with EC number 2.1.1.31 Full crystallographic information is available from OCA.
Reference
Insights into catalysis by a knotted TrmD tRNA methyltransferase., Elkins PA, Watts JM, Zalacain M, van Thiel A, Vitazka PR, Redlak M, Andraos-Selim C, Rastinejad F, Holmes WM, J Mol Biol. 2003 Nov 7;333(5):931-49. PMID:14583191
Page seeded by OCA on Thu Feb 21 14:26:40 2008
Categories: Escherichia coli, escherichia coli o6, escherichia coli o157:h7, and shigella flexneri | Single protein | TRNA (guanine-N(1)-)-methyltransferase | Andraos-Selim, C. | Elkins, P A. | Holmes, W M. | Rastinejad, F. | Redlak, M. | Thiel, A Van. | Vitaszka, P R. | Watts, J M. | Zalacain, M. | SAH | Adomet | Knot | Methyltransferase | S-adenosylmethionine | Spou | Spout
