2q2k
From Proteopedia
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| - | [[Image:2q2k.jpg|left|200px]] | + | [[Image:2q2k.jpg|left|200px]] |
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| - | '''Structure of nucleic-acid binding protein''' | + | {{Structure |
| + | |PDB= 2q2k |SIZE=350|CAPTION= <scene name='initialview01'>2q2k</scene>, resolution 3.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of nucleic-acid binding protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2Q2K is a [ | + | 2Q2K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q2K OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18097417 18097417] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: segregation]] | [[Category: segregation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:20:48 2008'' |
Revision as of 16:20, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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