1if0: Difference between revisions

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New page: left|200px<br /><applet load="1if0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1if0, resolution 12.Å" /> '''PSEUDO-ATOMIC MODEL O...
 
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[[Image:1if0.gif|left|200px]]<br /><applet load="1if0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1if0.gif|left|200px]]<br /><applet load="1if0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1if0, resolution 12.&Aring;" />
caption="1if0, resolution 12.&Aring;" />
'''PSEUDO-ATOMIC MODEL OF BACTERIOPHAGE HK97 PROCAPSID (PROHEAD II)'''<br />
'''PSEUDO-ATOMIC MODEL OF BACTERIOPHAGE HK97 PROCAPSID (PROHEAD II)'''<br />


==Overview==
==Overview==
Large-scale conformational changes transform viral precursors into, infectious virions. The structure of bacteriophage HK97 capsid, Head-II, was recently solved by crystallography, revealing a catenated cross-linked, topology. We have visualized its precursor, Prohead-II, by cryoelectron, microscopy and modeled the conformational change by appropriately adapting, Head-II. Rigid-body rotations ( approximately 40 degrees) cause switching, to an entirely different set of interactions; in addition, two motifs, undergo refolding. These changes stabilize the capsid by increasing the, surface area buried at interfaces and bringing the cross-link-forming, residues, initially approximately 40 angstroms apart, close together. The, inner surface of Prohead-II is negatively charged, suggesting that the, transition is triggered electrostatically by DNA packaging.
Large-scale conformational changes transform viral precursors into infectious virions. The structure of bacteriophage HK97 capsid, Head-II, was recently solved by crystallography, revealing a catenated cross-linked topology. We have visualized its precursor, Prohead-II, by cryoelectron microscopy and modeled the conformational change by appropriately adapting Head-II. Rigid-body rotations ( approximately 40 degrees) cause switching to an entirely different set of interactions; in addition, two motifs undergo refolding. These changes stabilize the capsid by increasing the surface area buried at interfaces and bringing the cross-link-forming residues, initially approximately 40 angstroms apart, close together. The inner surface of Prohead-II is negatively charged, suggesting that the transition is triggered electrostatically by DNA packaging.


==About this Structure==
==About this Structure==
1IF0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_hk620 Enterobacteria phage hk620]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IF0 OCA].  
1IF0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_hk620 Enterobacteria phage hk620]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IF0 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cheng, N.]]
[[Category: Cheng, N.]]
[[Category: Conway, J.F.]]
[[Category: Conway, J F.]]
[[Category: Duda, R.L.]]
[[Category: Duda, R L.]]
[[Category: Hendrix, R.W.]]
[[Category: Hendrix, R W.]]
[[Category: Johnson, J.E.]]
[[Category: Johnson, J E.]]
[[Category: Steven, A.C.]]
[[Category: Steven, A C.]]
[[Category: Wikoff, W.R.]]
[[Category: Wikoff, W R.]]
[[Category: bacteriophage]]
[[Category: bacteriophage]]
[[Category: capsid]]
[[Category: capsid]]
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[[Category: virus]]
[[Category: virus]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:21:15 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:13 2008''