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2jub

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(New page: 200px<br /><applet load="2jub" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jub" /> '''Solution structure of IPI*'''<br /> ==Overv...)
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==Overview==
==Overview==
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Phage T4 protects its DNA from the two-gene-encoded gmrS/gmrD, (glucose-modified hydroxymethylcytosine restriction endonuclease) CT of, pathogenic Escherichia coli, CT596, by injecting several hundred copies of, the 76-amino-acid-residue nuclease inhibitor, IPI*, into the infected, host. Here, the three-dimensional solution structure of mature IPI* is, reported as determined by nuclear magnetic resonance techniques using 1290, experimental nuclear Overhauser effect and dipolar coupling constraints (, approximately 17 constraints per residue). Close examination of this, oblate-shaped protein structure reveals a novel fold consisting of two, small beta-sheets (beta1: B1 and B2; beta2: B3-B5) flanked at the N- and, C-termini by alpha-helices (H1 and H2). Such a fold is very compact in, shape and allows ejection of IPI* through the narrow 30-A portal and tail, tube apertures of the virion without unfolding. Structural and dynamic, measurements identify an exposed hydrophobic knob that is a putative, gmrS/gmrD-binding site. A single gene from the uropathogenic E. coli, UT189, which codes for a gmrS/gmrD-like UT fusion enzyme (with, approximately 90% identity to the heterodimeric CT enzyme), has evolved, IPI* inhibitor immunity. Analysis of the gmrS/gmrD restriction, endonuclease enzyme family and its IPI* family phage antagonists reveals, an evolutionary pathway that has elaborated a surprisingly diverse and, specifically fitted set of coevolving attack and defense structures.
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Phage T4 protects its DNA from the two-gene-encoded gmrS/gmrD (glucose-modified hydroxymethylcytosine restriction endonuclease) CT of pathogenic Escherichia coli, CT596, by injecting several hundred copies of the 76-amino-acid-residue nuclease inhibitor, IPI*, into the infected host. Here, the three-dimensional solution structure of mature IPI* is reported as determined by nuclear magnetic resonance techniques using 1290 experimental nuclear Overhauser effect and dipolar coupling constraints ( approximately 17 constraints per residue). Close examination of this oblate-shaped protein structure reveals a novel fold consisting of two small beta-sheets (beta1: B1 and B2; beta2: B3-B5) flanked at the N- and C-termini by alpha-helices (H1 and H2). Such a fold is very compact in shape and allows ejection of IPI* through the narrow 30-A portal and tail tube apertures of the virion without unfolding. Structural and dynamic measurements identify an exposed hydrophobic knob that is a putative gmrS/gmrD-binding site. A single gene from the uropathogenic E. coli UT189, which codes for a gmrS/gmrD-like UT fusion enzyme (with approximately 90% identity to the heterodimeric CT enzyme), has evolved IPI* inhibitor immunity. Analysis of the gmrS/gmrD restriction endonuclease enzyme family and its IPI* family phage antagonists reveals an evolutionary pathway that has elaborated a surprisingly diverse and specifically fitted set of coevolving attack and defense structures.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Restriction Endonuclease Inhibitor IPI* of Bacteriophage T4: A Novel Structure for a Dedicated Target., Rifat D, Wright NT, Varney KM, Weber DJ, Black LW, J Mol Biol. 2007 Nov 1;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18037438 18037438]
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Restriction endonuclease inhibitor IPI* of bacteriophage T4: a novel structure for a dedicated target., Rifat D, Wright NT, Varney KM, Weber DJ, Black LW, J Mol Biol. 2008 Jan 18;375(3):720-34. Epub 2007 Nov 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18037438 18037438]
[[Category: Enterobacteria phage tw28]]
[[Category: Enterobacteria phage tw28]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Black, L.W.]]
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[[Category: Black, L W.]]
[[Category: Rifat, D.]]
[[Category: Rifat, D.]]
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[[Category: Varney, K.M.]]
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[[Category: Varney, K M.]]
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[[Category: Weber, D.J.]]
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[[Category: Weber, D J.]]
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[[Category: Wright, N.T.]]
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[[Category: Wright, N T.]]
[[Category: endonuclease inhibitor]]
[[Category: endonuclease inhibitor]]
[[Category: ipi*]]
[[Category: ipi*]]
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[[Category: t4 phage]]
[[Category: t4 phage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:12:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:05:55 2008''

Revision as of 16:05, 21 February 2008


2jub

Drag the structure with the mouse to rotate

Solution structure of IPI*

Overview

Phage T4 protects its DNA from the two-gene-encoded gmrS/gmrD (glucose-modified hydroxymethylcytosine restriction endonuclease) CT of pathogenic Escherichia coli, CT596, by injecting several hundred copies of the 76-amino-acid-residue nuclease inhibitor, IPI*, into the infected host. Here, the three-dimensional solution structure of mature IPI* is reported as determined by nuclear magnetic resonance techniques using 1290 experimental nuclear Overhauser effect and dipolar coupling constraints ( approximately 17 constraints per residue). Close examination of this oblate-shaped protein structure reveals a novel fold consisting of two small beta-sheets (beta1: B1 and B2; beta2: B3-B5) flanked at the N- and C-termini by alpha-helices (H1 and H2). Such a fold is very compact in shape and allows ejection of IPI* through the narrow 30-A portal and tail tube apertures of the virion without unfolding. Structural and dynamic measurements identify an exposed hydrophobic knob that is a putative gmrS/gmrD-binding site. A single gene from the uropathogenic E. coli UT189, which codes for a gmrS/gmrD-like UT fusion enzyme (with approximately 90% identity to the heterodimeric CT enzyme), has evolved IPI* inhibitor immunity. Analysis of the gmrS/gmrD restriction endonuclease enzyme family and its IPI* family phage antagonists reveals an evolutionary pathway that has elaborated a surprisingly diverse and specifically fitted set of coevolving attack and defense structures.

About this Structure

2JUB is a Single protein structure of sequence from Enterobacteria phage tw28. Full crystallographic information is available from OCA.

Reference

Restriction endonuclease inhibitor IPI* of bacteriophage T4: a novel structure for a dedicated target., Rifat D, Wright NT, Varney KM, Weber DJ, Black LW, J Mol Biol. 2008 Jan 18;375(3):720-34. Epub 2007 Nov 1. PMID:18037438

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