2bpc | pdb_00002bpc
|
CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM
Overview
Structures of the 31-kilodalton catalytic domain of rat DNA polymerase, beta (pol beta) and the whole 39-kilodalton enzyme were determined at 2.3, and 3.6 angstrom resolution, respectively. The 31-kilodalton domain is, composed of fingers, palm, and thumb subdomains arranged to form a DNA, binding channel reminiscent of the polymerase domains of the Klenow, fragment of Escherichia coli DNA polymerase I, HIV-1 reverse, transcriptase, and bacteriophage T7 RNA polymerase. The amino-terminal, 8-kilodalton domain is attached to the fingers subdomain by a flexible, hinge. The two invariant aspartates found in all polymerase sequences and, implicated in catalytic activity have the same geometric arrangement, within structurally similar but topologically distinct palms, indicating, that the polymerases have maintained, or possibly re-evolved, a common, nucleotidyl transfer mechanism. The location of Mn2+ and deoxyadenosine, triphosphate in pol beta confirms the role of the invariant aspartates in, metal ion and deoxynucleoside triphosphate binding.
About this Structure
2BPC is a Single protein structure of sequence from Rattus norvegicus with MN as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism., Sawaya MR, Pelletier H, Kumar A, Wilson SH, Kraut J, Science. 1994 Jun 24;264(5167):1930-5. PMID:7516581
Page seeded by OCA on Wed Nov 21 08:52:00 2007
