This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1eqa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1eqa.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1eqa.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1eqa| PDB=1eqa | SCENE= }}
{{STRUCTURE_1eqa| PDB=1eqa | SCENE= }}
-
'''VACCINIA METHYLTRANSFERASE VP39 MUTANT E233Q COMPLEXED WITH M7G AND S-ADENOSYLHOMOCYSTEINE'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10377383}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10377383 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10377383}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Vaccinia]]
[[Category: Vaccinia]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:24:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:39:28 2008''

Revision as of 22:39, 30 June 2008

Image:1eqa.png

Template:STRUCTURE 1eqa

VACCINIA METHYLTRANSFERASE VP39 MUTANT E233Q COMPLEXED WITH M7G AND S-ADENOSYLHOMOCYSTEINE

Template:ABSTRACT PUBMED 10377383

About this Structure

1EQA is a Single protein structure of sequence from Vaccinia virus. 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 Tue Jul 1 01:39:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eqa"
Personal tools