1aq4: Difference between revisions

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[[Image:1aq4.gif|left|200px]]
[[Image:1aq4.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq4 OCA], [http://www.ebi.ac.uk/pdbsum/1aq4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aq4 RCSB]</span>
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'''STRUCTURE OF A MS2 COAT PROTEIN MUTANT IN COMPLEX WITH AN RNA OPERATOR'''
'''STRUCTURE OF A MS2 COAT PROTEIN MUTANT IN COMPLEX WITH AN RNA OPERATOR'''
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[[Category: Valegard, K.]]
[[Category: Valegard, K.]]
[[Category: Worm, L Liljas S Van Den.]]
[[Category: Worm, L Liljas S Van Den.]]
[[Category: complex (coat protein/rna),coat protein]]
[[Category: Icosahedral virus]]
[[Category: icosahedral virus]]
[[Category: Rna fragment]]
[[Category: rna fragment]]
[[Category: Rna-binding]]
[[Category: rna-binding]]
[[Category: Viral protein capsid]]
[[Category: viral protein capsid]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:34:18 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:18 2008''

Revision as of 10:34, 2 May 2008

File:1aq4.gif

Template:STRUCTURE 1aq4

STRUCTURE OF A MS2 COAT PROTEIN MUTANT IN COMPLEX WITH AN RNA OPERATOR


OverviewOverview

In MS2 assembly of phage particles results from an interaction between a coat protein dimer and a stem-loop of the RNA genome (the operator hairpin). Amino acid residues Thr45, which is universally conserved among the small RNA phages, and Thr59 are part of the specific RNA binding pocket and interact directly with the RNA; the former through a hydrogen bond, the latter through hydrophobic contacts. The crystal structures of MS2 protein capsids formed by mutants Thr45Ala and Thr59Ser, both with and without the 19 nt wild-type operator hairpin bound, are reported here. The RNA hairpin binds to these mutants in a similar way to its binding to wild-type protein. In a companion paper both mutants are shown to be deficient in RNA binding in an in vivo assay, but in vitro the equilibrium dissociation constant is significantly higher than wild-type for the Thr45Ala mutant. The change in binding affinity of the Thr45Ala mutant is probably a direct consequence of removal of direct hydrogen bonds between the protein and the RNA. The properties of the Thr59Ser mutant are more difficult to explain, but are consistent with a loss of non-polar contact.

About this StructureAbout this Structure

1AQ4 is a Single protein structure of sequence from Enterobacterio phage ms2. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments., van den Worm SH, Stonehouse NJ, Valegard K, Murray JB, Walton C, Fridborg K, Stockley PG, Liljas L, Nucleic Acids Res. 1998 Mar 1;26(5):1345-51. PMID:9469847 Page seeded by OCA on Fri May 2 10:34:18 2008

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