2alz
From Proteopedia
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Ternary Complex of hPoli with DNA and dCTP
Overview
Human DNA polymerase iota (hPoliota), a member of the Y family of DNA, polymerases, differs in remarkable ways from other DNA polymerases, incorporating correct nucleotides opposite template purines with a much, higher efficiency and fidelity than opposite template pyrimidines. We, present here the crystal structure of hPoliota bound to template G and, incoming dCTP, which reveals a G.C + Hoogsteen base pair in a DNA, polymerase active site. We show that the hPoliota active site has evolved, to favor Hoogsteen base pairing, wherein the template sugar is fixed in a, cavity that reduces the C1'-C1' distance across the nascent base pair from, approximately 10.5 A in other DNA polymerases to 8.6 A in hPoliota. The, rotation of G from anti to syn is then largely in response to this, curtailed C1'-C1' distance. A G.C+ Hoogsteen base pair suggests a specific, mechanism for hPoliota's ability to bypass N(2)-adducted guanines that, obstruct replication.
About this Structure
2ALZ is a Single protein structure of sequence from Homo sapiens with MG and DCP as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Human DNA polymerase iota incorporates dCTP opposite template G via a G.C + Hoogsteen base pair., Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK, Structure. 2005 Oct;13(10):1569-77. PMID:16216587
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