1eqa
From Proteopedia
(New page: 200px<br /><applet load="1eqa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqa, resolution 2.2Å" /> '''VACCINIA METHYLTRANSF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1eqa.gif|left|200px]]<br /><applet load="1eqa" size=" | + | [[Image:1eqa.gif|left|200px]]<br /><applet load="1eqa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eqa, resolution 2.2Å" /> | caption="1eqa, resolution 2.2Å" /> | ||
'''VACCINIA METHYLTRANSFERASE VP39 MUTANT E233Q COMPLEXED WITH M7G AND S-ADENOSYLHOMOCYSTEINE'''<br /> | '''VACCINIA METHYLTRANSFERASE VP39 MUTANT E233Q COMPLEXED WITH M7G AND S-ADENOSYLHOMOCYSTEINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined, by high resolution x-ray analysis, 10 structures | + | We have determined, by high resolution x-ray analysis, 10 structures comprising the mRNA cap-specific methyltransferase VP39 or specific mutants thereof in the presence of methylated nucleobase analogs (N1-methyladenine, N3-methyladenine, N1-methylcytosine, N3-methylcytosine) and their unmethylated counterparts, or nucleoside N7-methylguanosine. Together with solution affinity studies and previous crystallographic data for N7-methylguanosine and its phosphorylated derivatives, these data demonstrate that only methylated, positively charged bases are bound, indicating that their enhanced stacking with two aromatic side chains of VP39 (Tyr 22 and Phe 180) plays a dominant role in cap recognition. Four key features characterize this stacking interaction: (i) near perfect parallel alignment between the sandwiched methylated bases and aromatic side chains, (ii) substantial areas of overlap in the two-stacked rings, (iii) a 3.4-A interplanar spacing within the overlapping region, and (iv) positive charge in the heterocyclic nucleobase. |
==About this Structure== | ==About this Structure== | ||
| - | 1EQA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus] with SAH and MG7 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] Full crystallographic information is available from [http:// | + | 1EQA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus] with <scene name='pdbligand=SAH:'>SAH</scene> and <scene name='pdbligand=MG7:'>MG7</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQA OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vaccinia virus]] | [[Category: Vaccinia virus]] | ||
| - | [[Category: Gershon, P | + | [[Category: Gershon, P D.]] |
| - | [[Category: Hodel, A | + | [[Category: Hodel, A E.]] |
[[Category: Hu, G.]] | [[Category: Hu, G.]] | ||
| - | [[Category: Quiocho, F | + | [[Category: Quiocho, F A.]] |
[[Category: MG7]] | [[Category: MG7]] | ||
[[Category: SAH]] | [[Category: SAH]] | ||
| Line 30: | Line 30: | ||
[[Category: vaccinia]] | [[Category: vaccinia]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:26 2008'' |
Revision as of 10:30, 21 February 2008
|
VACCINIA METHYLTRANSFERASE VP39 MUTANT E233Q COMPLEXED WITH M7G AND S-ADENOSYLHOMOCYSTEINE
Overview
We have determined, by high resolution x-ray analysis, 10 structures comprising the mRNA cap-specific methyltransferase VP39 or specific mutants thereof in the presence of methylated nucleobase analogs (N1-methyladenine, N3-methyladenine, N1-methylcytosine, N3-methylcytosine) and their unmethylated counterparts, or nucleoside N7-methylguanosine. Together with solution affinity studies and previous crystallographic data for N7-methylguanosine and its phosphorylated derivatives, these data demonstrate that only methylated, positively charged bases are bound, indicating that their enhanced stacking with two aromatic side chains of VP39 (Tyr 22 and Phe 180) plays a dominant role in cap recognition. Four key features characterize this stacking interaction: (i) near perfect parallel alignment between the sandwiched methylated bases and aromatic side chains, (ii) substantial areas of overlap in the two-stacked rings, (iii) a 3.4-A interplanar spacing within the overlapping region, and (iv) positive charge in the heterocyclic nucleobase.
About this Structure
1EQA is a Single protein structure of sequence from Vaccinia virus with and as ligands. Active as Polynucleotide adenylyltransferase, with EC number 2.7.7.19 Full crystallographic information is available from OCA.
Reference
mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains., Hu G, Gershon PD, Hodel AE, Quiocho FA, Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7149-54. PMID:10377383
Page seeded by OCA on Thu Feb 21 12:30:26 2008
Categories: Polynucleotide adenylyltransferase | Single protein | Vaccinia virus | Gershon, P D. | Hodel, A E. | Hu, G. | Quiocho, F A. | MG7 | SAH | Complex (transferase/rna cap analog) | Methylated guanosine | Methyltransferase | Mrna processing | Poly(a) polymerase | Rna cap analog | Transcription | Transferase | Vaccinia
