1gvn
From Proteopedia
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==Overview== | ==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 .. | + | 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== | ||
| - | 1GVN is a | + | 1GVN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: SOB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GVN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: postsegregational killing system]] | [[Category: postsegregational killing system]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:45:06 2007'' |
Revision as of 12:39, 5 November 2007
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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 SO4 as ligand. Structure known Active Site: SOB. 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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