1gvn

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==Overview==
==Overview==
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Programmed cell death in prokaryotes is frequently found as, postsegregational killing. It relies on antitoxin/toxin systems that, secure stable inheritance of low and medium copy number plasmids during, cell division and kill cells that have lost the plasmid. The, broad-host-range, low-copy-number plasmid pSM19035 from Streptococcus, pyogenes carries the genes encoding the antitoxin/toxin system, epsilon/zeta and antibiotic resistance proteins, among others. The crystal, structure of the biologically nontoxic epsilon(2)zeta(2) protein complex, at a 1.95-A resolution and site-directed mutagenesis showed that free zeta, acts as phosphotransferase by using ATPGTP. In epsilon(2)zeta(2), the, toxin zeta is inactivated because the N-terminal helix of the antitoxin, epsilon blocks the ATPGTP-binding site. To our knowledge, this is the, first prokaryotic postsegregational killing system that has been entirely, structurally characterized.
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Programmed cell death in prokaryotes is frequently found as postsegregational killing. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid. The broad-host-range, low-copy-number plasmid pSM19035 from Streptococcus pyogenes carries the genes encoding the antitoxin/toxin system epsilon/zeta and antibiotic resistance proteins, among others. The crystal structure of the biologically nontoxic epsilon(2)zeta(2) protein complex at a 1.95-A resolution and site-directed mutagenesis showed that free zeta acts as phosphotransferase by using ATPGTP. In epsilon(2)zeta(2), the toxin zeta is inactivated because the N-terminal helix of the antitoxin epsilon blocks the ATPGTP-binding site. To our knowledge, this is the first prokaryotic postsegregational killing system that has been entirely structurally characterized.
==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
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[[Category: Alonso, J.C.]]
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[[Category: Alonso, J C.]]
[[Category: Meinhart, A.]]
[[Category: Meinhart, A.]]
[[Category: Saenger, W.]]
[[Category: Saenger, W.]]
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[[Category: postsegregational killing system]]
[[Category: postsegregational killing system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:43:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:29 2008''

Revision as of 10:54, 21 February 2008


1gvn, resolution 1.95Å

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CRYSTAL STRUCTURE OF THE PLASMID MAINTENANCE SYSTEM EPSILON/ZETA: MEACHNISM OF TOXIN INACTIVATION AND TOXIN FUNCTION

Overview

Programmed cell death in prokaryotes is frequently found as postsegregational killing. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid. The broad-host-range, low-copy-number plasmid pSM19035 from Streptococcus pyogenes carries the genes encoding the antitoxin/toxin system epsilon/zeta and antibiotic resistance proteins, among others. The crystal structure of the biologically nontoxic epsilon(2)zeta(2) protein complex at a 1.95-A resolution and site-directed mutagenesis showed that free zeta acts as phosphotransferase by using ATPGTP. In epsilon(2)zeta(2), the toxin zeta is inactivated because the N-terminal helix of the antitoxin epsilon blocks the ATPGTP-binding site. To our knowledge, this is the first prokaryotic postsegregational killing system that has been entirely structurally characterized.

About this Structure

1GVN is a Protein complex structure of sequences from Streptococcus pyogenes with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structure of the plasmid maintenance system epsilon/zeta: functional mechanism of toxin zeta and inactivation by epsilon 2 zeta 2 complex formation., Meinhart A, Alonso JC, Strater N, Saenger W, Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1661-6. Epub 2003 Feb 5. PMID:12571357

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