2q2k

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==Overview==
==Overview==
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The stable inheritance of genetic material depends on accurate DNA, partition. Plasmids serve as tractable model systems to study DNA, segregation because they require only a DNA centromere, a, centromere-binding protein and a force-generating ATPase. The centromeres, of partition (par) systems typically consist of a tandem arrangement of, direct repeats. The best-characterized par system contains a, centromere-binding protein called ParR and an ATPase called ParM. In the, first step of segregation, multiple ParR proteins interact with the, centromere repeats to form a large nucleoprotein complex of unknown, structure called the segrosome, which binds ParM filaments. pSK41 ParR, binds a centromere consisting of multiple 20-base-pair (bp) tandem repeats, to mediate both transcription autoregulation and segregation. Here we, report the structure of the pSK41 segrosome revealed in the crystal, structure of a ParR-DNA complex. In the crystals, the 20-mer tandem, repeats stack pseudo-continuously to generate the full-length centromere, with the ribbon-helix-helix (RHH) fold of ParR binding successive DNA, repeats as dimer-of-dimers. Remarkably, the dimer-of-dimers assemble in a, continuous protein super-helical array, wrapping the DNA about its, positive convex surface to form a large segrosome with an open, solenoid-shaped structure, suggesting a mechanism for ParM capture and, subsequent plasmid segregation.
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The stable inheritance of genetic material depends on accurate DNA partition. Plasmids serve as tractable model systems to study DNA segregation because they require only a DNA centromere, a centromere-binding protein and a force-generating ATPase. The centromeres of partition (par) systems typically consist of a tandem arrangement of direct repeats. The best-characterized par system contains a centromere-binding protein called ParR and an ATPase called ParM. In the first step of segregation, multiple ParR proteins interact with the centromere repeats to form a large nucleoprotein complex of unknown structure called the segrosome, which binds ParM filaments. pSK41 ParR binds a centromere consisting of multiple 20-base-pair (bp) tandem repeats to mediate both transcription autoregulation and segregation. Here we report the structure of the pSK41 segrosome revealed in the crystal structure of a ParR-DNA complex. In the crystals, the 20-mer tandem repeats stack pseudo-continuously to generate the full-length centromere with the ribbon-helix-helix (RHH) fold of ParR binding successive DNA repeats as dimer-of-dimers. Remarkably, the dimer-of-dimers assemble in a continuous protein super-helical array, wrapping the DNA about its positive convex surface to form a large segrosome with an open, solenoid-shaped structure, suggesting a mechanism for ParM capture and subsequent plasmid segregation.
==About this Structure==
==About this Structure==
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[[Category: Firth, N.]]
[[Category: Firth, N.]]
[[Category: Glover, T.]]
[[Category: Glover, T.]]
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[[Category: Schumacher, M.A.]]
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[[Category: Schumacher, M A.]]
[[Category: EPE]]
[[Category: EPE]]
[[Category: dna binding protein/dna complex]]
[[Category: dna binding protein/dna complex]]
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[[Category: segregation]]
[[Category: segregation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:14:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:35:29 2008''

Revision as of 16:35, 21 February 2008


2q2k, resolution 3.00Å

Drag the structure with the mouse to rotate

Structure of nucleic-acid binding protein

Overview

The stable inheritance of genetic material depends on accurate DNA partition. Plasmids serve as tractable model systems to study DNA segregation because they require only a DNA centromere, a centromere-binding protein and a force-generating ATPase. The centromeres of partition (par) systems typically consist of a tandem arrangement of direct repeats. The best-characterized par system contains a centromere-binding protein called ParR and an ATPase called ParM. In the first step of segregation, multiple ParR proteins interact with the centromere repeats to form a large nucleoprotein complex of unknown structure called the segrosome, which binds ParM filaments. pSK41 ParR binds a centromere consisting of multiple 20-base-pair (bp) tandem repeats to mediate both transcription autoregulation and segregation. Here we report the structure of the pSK41 segrosome revealed in the crystal structure of a ParR-DNA complex. In the crystals, the 20-mer tandem repeats stack pseudo-continuously to generate the full-length centromere with the ribbon-helix-helix (RHH) fold of ParR binding successive DNA repeats as dimer-of-dimers. Remarkably, the dimer-of-dimers assemble in a continuous protein super-helical array, wrapping the DNA about its positive convex surface to form a large segrosome with an open, solenoid-shaped structure, suggesting a mechanism for ParM capture and subsequent plasmid segregation.

About this Structure

2Q2K is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.

Reference

Segrosome structure revealed by a complex of ParR with centromere DNA., Schumacher MA, Glover TC, Brzoska AJ, Jensen SO, Dunham TD, Skurray RA, Firth N, Nature. 2007 Dec 20;450(7173):1268-71. PMID:18097417

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