3b39
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:3b39.jpg|left|200px]] | [[Image:3b39.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_3b39", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_3b39| PDB=3b39 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Structure of the DnaG primase catalytic domain bound to ssDNA''' | '''Structure of the DnaG primase catalytic domain bound to ssDNA''' | ||
| Line 28: | Line 25: | ||
[[Category: Corn, J E.]] | [[Category: Corn, J E.]] | ||
[[Category: Pelton, J G.]] | [[Category: Pelton, J G.]] | ||
| - | [[Category: | + | [[Category: Dna replication]] |
| - | [[Category: | + | [[Category: Dna-directed rna polymerase]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Nucleotidyltransferase]] |
| - | [[Category: | + | [[Category: Primosome]] |
| - | [[Category: | + | [[Category: Protein-dna complex]] |
| - | [[Category: | + | [[Category: Toprim fold]] |
| - | [[Category: | + | [[Category: Transcription]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | [[Category: | + | [[Category: Transferase/dna complex]] |
| - | [[Category: | + | [[Category: Zinc]] |
| - | [[Category: | + | [[Category: Zinc-finger]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:21:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:21, 4 May 2008
Structure of the DnaG primase catalytic domain bound to ssDNA
Overview
Primases are essential RNA polymerases required for the initiation of DNA replication, lagging strand synthesis and replication restart. Many aspects of primase function remain unclear, including how the enzyme associates with a moving nucleic acid strand emanating from a helicase and orients primers for handoff to replisomal components. Using a new screening method to trap transient macromolecular interactions, we determined the structure of the Escherichia coli DnaG primase catalytic domain bound to single-stranded DNA. The structure reveals an unanticipated binding site that engages nucleic acid in two distinct configurations, indicating that it serves as a nonspecific capture and tracking locus for template DNA. Bioinformatic and biochemical analyses show that this evolutionarily constrained region enforces template polarity near the active site and is required for primase function. Together, our findings reverse previous proposals for primer-template orientation and reconcile disparate studies to re-evaluate replication fork organization.
About this Structure
3B39 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Identification of a DNA primase template tracking site redefines the geometry of primer synthesis., Corn JE, Pelton JG, Berger JM, Nat Struct Mol Biol. 2008 Feb;15(2):163-9. Epub 2008 Jan 13. PMID:18193061 Page seeded by OCA on Sun May 4 20:21:16 2008
Categories: Escherichia coli | Protein complex | Berger, J M. | Corn, J E. | Pelton, J G. | Dna replication | Dna-directed rna polymerase | Metal-binding | Nucleotidyltransferase | Primosome | Protein-dna complex | Toprim fold | Transcription | Transferase | Transferase/dna complex | Zinc | Zinc-finger
