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

OverviewOverview

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.

About this StructureAbout this Structure

1CKO is a Single protein structure of sequence from Paramecium bursaria chlorella virus 1 with and as ligands. Active as mRNA guanylyltransferase, with EC number 2.7.7.50 Full crystallographic information is available from OCA.

ReferenceReference

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

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 '''STRUCTURE OF MRNA CAPPING ENZYME IN COMPLEX WITH THE CAP ANALOG GPPPG'''<br />
 ==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.
+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.
 ==About this Structure==
-CKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1] with ZN and GP3 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/mRNA_guanylyltransferase mRNA guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.50 2.7.7.50] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CKO OCA].
+CKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GP3:'>GP3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/mRNA_guanylyltransferase mRNA guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.50 2.7.7.50] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKO OCA].
 ==Reference==
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 [[Category: mRNA guanylyltransferase]]
 [[Category: Hakansson, K.]]
-[[Category: Wigley, D.B.]]
+[[Category: Wigley, D B.]]
 [[Category: GP3]]
 [[Category: ZN]]
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 [[Category: nucleotidyltransferase]]
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