1zdh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1zdh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zdh, resolution 2.700&Aring;" /> '''MS2 COAT PROTEIN/RN...)
Line 1: Line 1:
-
[[Image:1zdh.gif|left|200px]]<br /><applet load="1zdh" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1zdh.gif|left|200px]]<br /><applet load="1zdh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zdh, resolution 2.700&Aring;" />
caption="1zdh, resolution 2.700&Aring;" />
'''MS2 COAT PROTEIN/RNA COMPLEX'''<br />
'''MS2 COAT PROTEIN/RNA COMPLEX'''<br />
==Overview==
==Overview==
-
Crystal structures of two complexes between recombinant MS2 capsids and, RNA operator fragments have been determined at 2.7 A resolution. The coat, protein of the RNA bacteriophage MS2 is bifunctional; it forms the, icosahedral virus shell to protect the viral nucleic acid and it acts as a, translational repressor by binding with high specificity to a unique site, on the RNA, a single stem-loop structure, containing the initiation codon, of the gene for the viral replicase. In order to determine the structure, of these protein-RNA complexes, we have used chemically synthesized, variants of the stem-loop fragment and soaked them into crystals of, recombinant capsids. The RNA stem-loop, as bound to the protein, forms a, crescent-like structure and interacts with the surface of the beta-sheet, of a coat protein dimer. It makes protein contacts with seven phosphate, groups on the 5' side of the stem-loop, with a pyrimidine base at position, -5, which stacks onto a tyrosine, and with two exposed adenine bases, one, in the loop and one at a bulge in the stem. Replacement of the wild-type, uridine with a cytosine at position -5 increases the affinity of the RNA, to the dimer significantly. The complex with RNA stem-loop having cytosine, at this position differs from that of the wild-type complex mainly by, having one extra intramolecular RNA interaction and one extra, water-mediated hydrogen bond.
+
Crystal structures of two complexes between recombinant MS2 capsids and RNA operator fragments have been determined at 2.7 A resolution. The coat protein of the RNA bacteriophage MS2 is bifunctional; it forms the icosahedral virus shell to protect the viral nucleic acid and it acts as a translational repressor by binding with high specificity to a unique site on the RNA, a single stem-loop structure, containing the initiation codon of the gene for the viral replicase. In order to determine the structure of these protein-RNA complexes, we have used chemically synthesized variants of the stem-loop fragment and soaked them into crystals of recombinant capsids. The RNA stem-loop, as bound to the protein, forms a crescent-like structure and interacts with the surface of the beta-sheet of a coat protein dimer. It makes protein contacts with seven phosphate groups on the 5' side of the stem-loop, with a pyrimidine base at position -5, which stacks onto a tyrosine, and with two exposed adenine bases, one in the loop and one at a bulge in the stem. Replacement of the wild-type uridine with a cytosine at position -5 increases the affinity of the RNA to the dimer significantly. The complex with RNA stem-loop having cytosine at this position differs from that of the wild-type complex mainly by having one extra intramolecular RNA interaction and one extra water-mediated hydrogen bond.
==About this Structure==
==About this Structure==
-
1ZDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacterio_phage_ms2 Enterobacterio phage ms2]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZDH OCA].
+
1ZDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacterio_phage_ms2 Enterobacterio phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDH OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Enterobacterio phage ms2]]
[[Category: Enterobacterio phage ms2]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: K.Valegard,S.Van Den Worm,L.Liljas]]
+
[[Category: K Valegard,S Van Den Worm,L Liljas]]
[[Category: coat protein]]
[[Category: coat protein]]
[[Category: complex (coat protein/rna)]]
[[Category: complex (coat protein/rna)]]
Line 21: Line 21:
[[Category: viral protein capsid]]
[[Category: viral protein capsid]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:24:00 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:29 2008''

Revision as of 14:14, 21 February 2008


1zdh, resolution 2.700Å

Drag the structure with the mouse to rotate

MS2 COAT PROTEIN/RNA COMPLEX

Overview

Crystal structures of two complexes between recombinant MS2 capsids and RNA operator fragments have been determined at 2.7 A resolution. The coat protein of the RNA bacteriophage MS2 is bifunctional; it forms the icosahedral virus shell to protect the viral nucleic acid and it acts as a translational repressor by binding with high specificity to a unique site on the RNA, a single stem-loop structure, containing the initiation codon of the gene for the viral replicase. In order to determine the structure of these protein-RNA complexes, we have used chemically synthesized variants of the stem-loop fragment and soaked them into crystals of recombinant capsids. The RNA stem-loop, as bound to the protein, forms a crescent-like structure and interacts with the surface of the beta-sheet of a coat protein dimer. It makes protein contacts with seven phosphate groups on the 5' side of the stem-loop, with a pyrimidine base at position -5, which stacks onto a tyrosine, and with two exposed adenine bases, one in the loop and one at a bulge in the stem. Replacement of the wild-type uridine with a cytosine at position -5 increases the affinity of the RNA to the dimer significantly. The complex with RNA stem-loop having cytosine at this position differs from that of the wild-type complex mainly by having one extra intramolecular RNA interaction and one extra water-mediated hydrogen bond.

About this Structure

1ZDH is a Single protein structure of sequence from Enterobacterio phage ms2. Full crystallographic information is available from OCA.

Reference

The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions., Valegard K, Murray JB, Stonehouse NJ, van den Worm S, Stockley PG, Liljas L, J Mol Biol. 1997 Aug 1;270(5):724-38. PMID:9245600

Page seeded by OCA on Thu Feb 21 16:14:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools