2r6a
From Proteopedia
Crystal Form BH1
Structural highlights
Function[DNAG_GEOSE] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase.,Bailey S, Eliason WK, Steitz TA Science. 2007 Oct 19;318(5849):459-63. PMID:17947583[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Atcc 12980 | Large Structures | Bailey, S | Eliason, W K | Steitz, T A | Dnab | Dnag | Helicase | Primase | Replication
