1gvn

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[[Image:1gvn.jpg|left|200px]]<br /><applet load="1gvn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gvn.jpg|left|200px]]
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caption="1gvn, resolution 1.95&Aring;" />
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'''CRYSTAL STRUCTURE OF THE PLASMID MAINTENANCE SYSTEM EPSILON/ZETA: MEACHNISM OF TOXIN INACTIVATION AND TOXIN FUNCTION'''<br />
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{{Structure
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|PDB= 1gvn |SIZE=350|CAPTION= <scene name='initialview01'>1gvn</scene>, resolution 1.95&Aring;
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|SITE= <scene name='pdbsite=SOB:So4+Binding+Site+For+Chain+D'>SOB</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE PLASMID MAINTENANCE SYSTEM EPSILON/ZETA: MEACHNISM OF TOXIN INACTIVATION AND TOXIN FUNCTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=SOB:So4+Binding+Site+For+Chain+D'>SOB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVN OCA].
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1GVN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVN OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12571357 12571357]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12571357 12571357]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
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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 Thu Feb 21 12:54:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:34 2008''

Revision as of 09:28, 20 March 2008


PDB ID 1gvn

Drag the structure with the mouse to rotate
, resolution 1.95Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



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. 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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