3SV4

Crystal structure of the large fragment of DNA polymerase I from Thermus Aquaticus in an open binary complex with dT as templating nucleobase

Summary for 3SV4

• Entry DOI: 10.2210/pdb3sv4/pdb
• Related: 3SV3 3SYZ 3SZ2 4KTQ
• Descriptor: DNA polymerase I, thermostable, (5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*GP*CP*(DOC))-3'), (5'-D(*AP*AP*AP*TP*GP*GP*CP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3'), ... (6 entities in total)
• Functional Keywords: dna polymerase, transferase-dna complex, transferase/dna
• Biological source: Thermus aquaticus; More
• Total number of polymer chains: 3
• Total formula weight: 69980.68

Authors

Betz, K.,Diederichs, K.,Marx, A. (deposition date: 2011-07-12, release date: 2012-06-06, Last modification date: 2023-09-13)

Primary citation

Betz, K.,Malyshev, D.A.,Lavergne, T.,Welte, W.,Diederichs, K.,Dwyer, T.J.,Ordoukhanian, P.,Romesberg, F.E.,Marx, A.
KlenTaq polymerase replicates unnatural base pairs by inducing a Watson-Crick geometry.
Nat.Chem.Biol., 8:612-614, 2012

PubMed Abstract: Many candidate unnatural DNA base pairs have been developed, but some of the best-replicated pairs adopt intercalated structures in free DNA that are difficult to reconcile with known mechanisms of polymerase recognition. Here we present crystal structures of KlenTaq DNA polymerase at different stages of replication for one such pair, dNaM-d5SICS, and show that efficient replication results from the polymerase itself, inducing the required natural-like structure.

PubMed: 22660438
DOI: 10.1038/nchembio.966

Experimental method

X-RAY DIFFRACTION (1.99 Å)