1bpd
From Proteopedia
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[[Image:1bpd.gif|left|200px]] | [[Image:1bpd.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM''' | '''CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM''' | ||
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[[Category: Sawaya, M R.]] | [[Category: Sawaya, M R.]] | ||
[[Category: Wilson, S H.]] | [[Category: Wilson, S H.]] | ||
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Revision as of 08:47, 2 May 2008
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
1BPD is a Single protein structure of sequence from Rattus norvegicus. 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 Fri May 2 11:47:49 2008