2fll
From Proteopedia
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Ternary complex of human DNA polymerase iota with DNA and dTTP
Overview
Substrate-induced conformational change of the protein is the linchpin of, enzymatic reactions. Replicative DNA polymerases, for example, convert, from an open to a closed conformation in response to dNTP binding. Human, DNA polymerase-iota (hPoliota), a member of the Y family of DNA, polymerases, differs strikingly from other polymerases in its much higher, proficiency and fidelity for nucleotide incorporation opposite template, purines than opposite template pyrimidines. We present here a, crystallographic analysis of hPoliota binary complexes, which together, with the ternary complexes show that, contrary to replicative DNA, polymerases, the DNA, and not the polymerase, undergoes the primary, substrate-induced conformational change. The incoming dNTP "pushes", templates A and G from the anti to the syn conformation dictated by a, rigid hPoliota active site. Together, the structures posit a mechanism for, template selection wherein dNTP binding induces a conformational switch in, template purines for productive Hoogsteen base pairing.
About this Structure
2FLL is a Single protein structure of sequence from Homo sapiens with MG and TTP as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
An incoming nucleotide imposes an anti to syn conformational change on the templating purine in the human DNA polymerase-iota active site., Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK, Structure. 2006 Apr;14(4):749-55. PMID:16615915
Page seeded by OCA on Mon Nov 12 22:07:00 2007
