3bh0: Difference between revisions

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[[Image:3bh0.jpg|left|200px]]
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[[Image:3bh0.png|left|200px]]


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{{STRUCTURE_3bh0|  PDB=3bh0  |  SCENE=  }}  
{{STRUCTURE_3bh0|  PDB=3bh0  |  SCENE=  }}  


'''ATPase Domain of G40P'''
===ATPase Domain of G40P===




==Overview==
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Helicases are essential enzymes for DNA replication, a fundamental process in all living organisms. The DnaB family are hexameric replicative helicases that unwind duplex DNA and coordinate with RNA primase and other proteins at the replication fork in prokaryotes. Here, we report the full-length crystal structure of G40P, a DnaB family helicase. The hexamer complex reveals an unusual architectural feature and a new type of assembly mechanism. The hexamer has two tiers: a three-fold symmetric N-terminal tier and a six-fold symmetric C-terminal tier. Monomers with two different conformations, termed cis and trans, come together to provide a topological solution for the dual symmetry within a hexamer. Structure-guided mutational studies indicate an important role for the N-terminal tier in binding primase and regulating primase-mediated stimulation of helicase activity. This study provides insights into the structural and functional interplay between G40P helicase and DnaG primase.
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{{ABSTRACT_PUBMED_18157148}}


==About this Structure==
==About this Structure==
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[[Category: Helicase]]
[[Category: Helicase]]
[[Category: Replication]]
[[Category: Replication]]
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Revision as of 01:46, 28 July 2008

File:3bh0.png

Template:STRUCTURE 3bh0

ATPase Domain of G40P

Template:ABSTRACT PUBMED 18157148

About this Structure

3BH0 is a Single protein structure of sequence from Bacillus phage spp1. Full crystallographic information is available from OCA.

Reference

The structure of a DnaB-family replicative helicase and its interactions with primase., Wang G, Klein MG, Tokonzaba E, Zhang Y, Holden LG, Chen XS, Nat Struct Mol Biol. 2008 Jan;15(1):94-100. Epub 2007 Dec 23. PMID:18157148

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