1bms: Difference between revisions

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New page: left|200px<br /><applet load="1bms" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bms, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...
 
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'''CRYSTAL STRUCTURE OF MS2 CAPSIDS WITH MUTATIONS IN THE SUBUNIT FG LOOP'''<br />
'''CRYSTAL STRUCTURE OF MS2 CAPSIDS WITH MUTATIONS IN THE SUBUNIT FG LOOP'''<br />


==Overview==
==Overview==
The loop between the F and G beta strands (FG loop) of the bacteriophage, MS2 coat protein subunit forms inter-subunit contacts around the 5-fold, and 3-fold (quasi 6-fold) axes of the T=3 protein shell. In capsids, the, loop is found in two very different conformations, one in B subunits, which form the 5-fold contact, and one in A and C subunits, which form the, quasi 6-fold contact. One proline residue, Pro78, is strictly conserved in, the coat protein of all related bacteriophages, and in the case of MS2, this proline residue is preceded by a cis peptide bond in the B subunit., In order to probe the role of the FG loop in capsid assembly, we have, determined the crystal structures of two MS2 capsids, formed by coat, proteins with mutations at two positions in the FG loop, P78N or E76D., These mutants show conformational changes in the FG loops that explain the, reduced temperature stability of the capsids. The P78N mutant has a normal, trans peptide bond at position 78.
The loop between the F and G beta strands (FG loop) of the bacteriophage MS2 coat protein subunit forms inter-subunit contacts around the 5-fold and 3-fold (quasi 6-fold) axes of the T=3 protein shell. In capsids, the loop is found in two very different conformations, one in B subunits, which form the 5-fold contact, and one in A and C subunits, which form the quasi 6-fold contact. One proline residue, Pro78, is strictly conserved in the coat protein of all related bacteriophages, and in the case of MS2 this proline residue is preceded by a cis peptide bond in the B subunit. In order to probe the role of the FG loop in capsid assembly, we have determined the crystal structures of two MS2 capsids, formed by coat proteins with mutations at two positions in the FG loop, P78N or E76D. These mutants show conformational changes in the FG loops that explain the reduced temperature stability of the capsids. The P78N mutant has a normal trans peptide bond at position 78.


==About this Structure==
==About this Structure==
1BMS 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=1BMS OCA].  
1BMS 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=1BMS OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Liljas, L.]]
[[Category: Liljas, L.]]
[[Category: Stonehouse, N.J.]]
[[Category: Stonehouse, N J.]]
[[Category: bacteriophage coat protein]]
[[Category: bacteriophage coat protein]]
[[Category: icosahedral virus]]
[[Category: icosahedral virus]]


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Revision as of 12:57, 21 February 2008

File:1bms.gif


1bms, resolution 2.7Å

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CRYSTAL STRUCTURE OF MS2 CAPSIDS WITH MUTATIONS IN THE SUBUNIT FG LOOP

OverviewOverview

The loop between the F and G beta strands (FG loop) of the bacteriophage MS2 coat protein subunit forms inter-subunit contacts around the 5-fold and 3-fold (quasi 6-fold) axes of the T=3 protein shell. In capsids, the loop is found in two very different conformations, one in B subunits, which form the 5-fold contact, and one in A and C subunits, which form the quasi 6-fold contact. One proline residue, Pro78, is strictly conserved in the coat protein of all related bacteriophages, and in the case of MS2 this proline residue is preceded by a cis peptide bond in the B subunit. In order to probe the role of the FG loop in capsid assembly, we have determined the crystal structures of two MS2 capsids, formed by coat proteins with mutations at two positions in the FG loop, P78N or E76D. These mutants show conformational changes in the FG loops that explain the reduced temperature stability of the capsids. The P78N mutant has a normal trans peptide bond at position 78.

About this StructureAbout this Structure

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

ReferenceReference

Crystal structures of MS2 capsids with mutations in the subunit FG loop., Stonehouse NJ, Valegard K, Golmohammadi R, van den Worm S, Walton C, Stockley PG, Liljas L, J Mol Biol. 1996 Feb 23;256(2):330-9. PMID:8594200

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