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PDBsum entry 1zet

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Replication/DNA PDB id
1zet
Contents
Protein chain
388 a.a.
DNA/RNA
Ligands
TTP
Metals
_MG
Waters ×168

References listed in PDB file
Key reference
Title Dna polymerases: hoogsteen base-Pairing in DNA replication?
Author J.Wang.
Ref. Nature, 2005, 437, E6-7; discussion E7.
PubMed id 16163299
Abstract
Human polymerase-iota belongs to the error-prone Y family of polymerases, which frequently incorporate incorrect nucleotides during DNA replication but can efficiently bypass DNA lesions. On the basis of X-ray diffraction data, Nair et al. propose that Hoogsteen base-pairing is adopted by DNA during its replication by this enzyme. Here I re-examine their X-ray data and find that the electron density is very weak for a Hoogsteen base pair formed between a template adenine deoxyribonucleotide in the syn conformation and a deoxythymidine 5'-triphosphate (dTTP), and that the fit is better for a normal Watson-Crick base pair. As a guanine-cytosine (G-C) base pair has no potential to form a Hoogsteen base pair at physiological pH, Hoogsteen base-pairing is unlikely to be used in replication by this polymerase.
Secondary reference #1
Title Replication by human DNA polymerase-Iota occurs by hoogsteen base-Pairing.
Authors D.T.Nair, R.E.Johnson, S.Prakash, L.Prakash, A.K.Aggarwal.
Ref. Nature, 2004, 430, 377-380. [DOI no: 10.1038/nature02692]
PubMed id 15254543
Full text Abstract
Figure 1.
Figure 1: Structure of the hPol iota--DNA -dTTP ternary complex. The palm, fingers, thumb domains and the PAD in the two hPol molecules are shown in blue, yellow, orange and green, respectively. DNA is shown in grey and the incoming dTTP in red.
Figure 2.
Figure 2: Comparison between hPol iota-and Dpo4. a, Close-up views of the active sites of hPol and Dpo4. The fingers and palm domains and the PAD are shown in yellow, blue and green, respectively. The DNA is shown in grey, and the templating nucleotide and the incoming nucleotide (dTTP in hPol and ddADP in Dpo4) in red. The metal ion is dark blue. Highlighted and labelled are the catalytic residues (Asp 34, Asp 126 and Glu 127 in hPol and Asp 7, Asp 105 and Glu 106 in Dpo4), the dNTP-bonding residues (Tyr 39, Tyr 68, Arg 71 and Lys 214 in hPol and Tyr 12, Tyr 48, Arg 51 and Lys 159 in Dpo4), and the residues close to the templating base (Gln 59, Lys 60, Leu 62 and Val 64 in hPol and Val 32, Ala 42 and Ala 44 in Dpo4). Note that the templating base is in syn conformation in the hPol active site and in trans conformation in the Dpo4 active site. b, Close-up views of Hoogsteen base-pairing (dA dTTP) in the active site of hPol and Watson -Crick base-pairing (dT ddADP) in the active site of Dpo4. c, Close-up views of the nascent base pair fitting against the hPol and Dpo4 molecular surfaces. The residues apposed to the templating base are shown in grey and labelled on the molecular surface.
The above figures are reproduced from the cited reference with permission from Macmillan Publishers Ltd
PROCHECK
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