1ofu

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==Overview==
==Overview==
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SulA halts cell division in Escherichia coli by binding to the major, component of the division machinery FtsZ. We have solved the crystal, structure of SulA alone and in complex with FtsZ from Pseudomonas, aeruginosa. SulA is expressed when the SOS response is induced. This is a, mechanism to inhibit cell division and repair DNA in the event of DNA, damage. FtsZ is a tubulin-like protein that forms polymers, with the, active-site GTPase split across two monomers. One monomer provides the, GTP-binding site and the other, through its T7 loop nucleotide hydrolysis., Our structures show that SulA is a dimer, and that SulA inhibits cell, division neither by binding the nucleotide-binding site nor by inducing, conformational changes in FtsZ. Instead, SulA binds the T7 loop surface of, FtsZ, opposite the nucleotide-binding site, blocking polymer formation., These findings explain why GTP hydrolysis and polymer turnover are, required for SulA inhibition.
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SulA halts cell division in Escherichia coli by binding to the major component of the division machinery FtsZ. We have solved the crystal structure of SulA alone and in complex with FtsZ from Pseudomonas aeruginosa. SulA is expressed when the SOS response is induced. This is a mechanism to inhibit cell division and repair DNA in the event of DNA damage. FtsZ is a tubulin-like protein that forms polymers, with the active-site GTPase split across two monomers. One monomer provides the GTP-binding site and the other, through its T7 loop nucleotide hydrolysis. Our structures show that SulA is a dimer, and that SulA inhibits cell division neither by binding the nucleotide-binding site nor by inducing conformational changes in FtsZ. Instead, SulA binds the T7 loop surface of FtsZ, opposite the nucleotide-binding site, blocking polymer formation. These findings explain why GTP hydrolysis and polymer turnover are required for SulA inhibition.
==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Cordell, S.C.]]
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[[Category: Cordell, S C.]]
[[Category: Lowe, J.]]
[[Category: Lowe, J.]]
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[[Category: Robinson, E.J.H.]]
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[[Category: Robinson, E J.H.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: bacterial cell division inhibitor]]
[[Category: bacterial cell division inhibitor]]
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[[Category: sula protein]]
[[Category: sula protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:57:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:12 2008''

Revision as of 12:17, 21 February 2008


1ofu, resolution 2.1Å

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CRYSTAL STRUCTURE OF SULA:FTSZ FROM PSEUDOMONAS AERUGINOSA

Overview

SulA halts cell division in Escherichia coli by binding to the major component of the division machinery FtsZ. We have solved the crystal structure of SulA alone and in complex with FtsZ from Pseudomonas aeruginosa. SulA is expressed when the SOS response is induced. This is a mechanism to inhibit cell division and repair DNA in the event of DNA damage. FtsZ is a tubulin-like protein that forms polymers, with the active-site GTPase split across two monomers. One monomer provides the GTP-binding site and the other, through its T7 loop nucleotide hydrolysis. Our structures show that SulA is a dimer, and that SulA inhibits cell division neither by binding the nucleotide-binding site nor by inducing conformational changes in FtsZ. Instead, SulA binds the T7 loop surface of FtsZ, opposite the nucleotide-binding site, blocking polymer formation. These findings explain why GTP hydrolysis and polymer turnover are required for SulA inhibition.

About this Structure

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

Reference

Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ., Cordell SC, Robinson EJ, Lowe J, Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7889-94. Epub 2003 Jun 13. PMID:12808143

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