1WAJ

DNA POLYMERASE FROM BACTERIOPHAGE RB69

Summary for 1WAJ

• Entry DOI: 10.2210/pdb1waj/pdb
• Descriptor: DNA POLYMERASE, GUANOSINE-5'-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: nucleotidyltransferase, rb69 dna polymerase (gp43)
• Biological source: Enterobacteria phage RB69
• Total number of polymer chains: 1
• Total formula weight: 105106.38

Authors

Wang, J.,Satter, A.K.M.A.,Wang, C.C.,Karam, J.D.,Konigsberg, W.H.,Steitz, T.A. (deposition date: 1997-04-13, release date: 1998-01-14, Last modification date: 2024-02-14)

Primary citation

Wang, J.,Sattar, A.K.,Wang, C.C.,Karam, J.D.,Konigsberg, W.H.,Steitz, T.A.
Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69.
Cell(Cambridge,Mass.), 89:1087-1099, 1997

PubMed Abstract: The 2.8 A resolution crystal structure of the bacteriophage RB69 gp43, a member of the eukaryotic pol alpha family of replicative DNA polymerases, shares some similarities with other polymerases but shows many differences. Although its palm domain has the same topology as other polymerases, except rat DNA polymerase beta, one of the three carboxylates required for nucleotidyl transfer is located on a different beta strand. The structures of the fingers and thumb domains are unrelated to all other known polymerase structures. The editing 3'-5' exonuclease domain of gp43 is homologous to that of E. coli DNA polymerase I but lies on the opposite side of the polymerase active site. An extended structure-based alignment of eukaryotic DNA polymerase sequences provides structural insights that should be applicable to most eukaryotic DNA polymerases.

PubMed: 9215631
DOI: 10.1016/S0092-8674(00)80296-2

Experimental method

X-RAY DIFFRACTION (2.8 Å)