1if0

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(New page: 200px<br /><applet load="1if0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1if0, resolution 12.&Aring;" /> '''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"
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[[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==
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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.
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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==
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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].
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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.]]
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[[Category: Conway, J.F.]]
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[[Category: Conway, J F.]]
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[[Category: Duda, R.L.]]
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[[Category: Duda, R L.]]
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[[Category: Hendrix, R.W.]]
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[[Category: Hendrix, R W.]]
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[[Category: Johnson, J.E.]]
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[[Category: Johnson, J E.]]
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[[Category: Steven, A.C.]]
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[[Category: Steven, A C.]]
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[[Category: Wikoff, W.R.]]
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[[Category: Wikoff, W R.]]
[[Category: bacteriophage]]
[[Category: bacteriophage]]
[[Category: capsid]]
[[Category: capsid]]
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[[Category: virus]]
[[Category: virus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:21:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:13 2008''

Revision as of 11:11, 21 February 2008


1if0, resolution 12.Å

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PSEUDO-ATOMIC MODEL OF BACTERIOPHAGE HK97 PROCAPSID (PROHEAD II)

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.

About this Structure

1IF0 is a Single protein structure of sequence from Enterobacteria phage hk620. Full crystallographic information is available from OCA.

Reference

Virus maturation involving large subunit rotations and local refolding., Conway JF, Wikoff WR, Cheng N, Duda RL, Hendrix RW, Johnson JE, Steven AC, Science. 2001 Apr 27;292(5517):744-8. PMID:11326105

Page seeded by OCA on Thu Feb 21 13:11:13 2008

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