We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1cko

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cko.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1cko.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cko| PDB=1cko | SCENE= }}
{{STRUCTURE_1cko| PDB=1cko | SCENE= }}
-
'''STRUCTURE OF MRNA CAPPING ENZYME IN COMPLEX WITH THE CAP ANALOG GPPPG'''
+
===STRUCTURE OF MRNA CAPPING ENZYME IN COMPLEX WITH THE CAP ANALOG GPPPG===
-
==Overview==
+
<!--
-
Paramecium bursaria Chlorella virus PBCV-1 mRNA guanylyl transferase (capping enzyme) has been complexed with an mRNA cap analogue G[5']ppp[5']G and crystallized. The crystals belong to space group C2221 with unit cell dimensions a = 78.4 A, b = 164.1 A, c = 103.3 A, and diffraction data to 3.1 A has been collected by using synchrotron radiation. The structure has been solved by molecular replacement by using each of the two domains in the previously determined structure of the enzyme in complex with GTP. The conformation is open with respect to the active site cleft, and all contacts between enzyme and ligand are mediated by domain 1. One of the guanine bases is bound in the same pocket that is utilized by GTP. The conformation of the ligand positions the beta phosphate and the active site lysine on opposite sides of the alpha phosphate. This geometry is optimal for nucleophilic substitution reactions and has previously been found for GTP in the closed conformational form of the capping enzyme, where the lysine can be guanylylated upon treatment with excess manganese(II) ions. The remainder of the cap analogue runs along the conserved active site Lys82 Thr83 Asp84 Gly85 Ile86 Arg87 motif, and the second guanine, corresponding to the 5' RNA base, is stacked against the hydrophobic Ile86. The ligand displays approximate 2-fold symmetry with intramolecular hydrogen bonding between the 2' and 3' hydroxyls of the two ribose rings.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9465045}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9465045 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9465045}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Mrna]]
[[Category: Mrna]]
[[Category: Nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:50:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:52:48 2008''

Revision as of 17:52, 30 June 2008

Image:1cko.png

Template:STRUCTURE 1cko

STRUCTURE OF MRNA CAPPING ENZYME IN COMPLEX WITH THE CAP ANALOG GPPPG

Template:ABSTRACT PUBMED 9465045

About this Structure

1CKO is a Single protein structure of sequence from Paramecium bursaria chlorella virus 1. Full crystallographic information is available from OCA.

Reference

Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping., Hakansson K, Wigley DB, Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1505-10. PMID:9465045

Page seeded by OCA on Mon Jun 30 20:52:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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